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A0R2B1

- KGD_MYCS2

UniProt

A0R2B1 - KGD_MYCS2

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Protein

Multifunctional 2-oxoglutarate metabolism enzyme

Gene
kgd, sucA, MSMEG_5049, MSMEI_4922
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Shows three enzymatic activities that share a first common step, the attack of thiamine-PP on 2-oxoglutarate (alpha-ketoglutarate, KG), leading to the formation of an enamine-thiamine-PP intermediate upon decarboxylation. Thus, displays KGD activity, catalyzing the decarboxylation from five-carbon 2-oxoglutarate to four-carbon succinate semialdehyde (SSA). Also catalyzes C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA), which spontaneously decarboxylates to form 5-hydroxylevulinate (HLA). And is also a component of the 2-oxoglutarate dehydrogenase (ODH) complex, that catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO2. The KG decarboxylase and KG dehydrogenase reactions provide two alternative, tightly regulated, pathways connecting the oxidative and reductive branches of the TCA cycle.2 Publications

Catalytic activityi

2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2.1 Publication
2-oxoglutarate = succinate semialdehyde + CO2.1 Publication
2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2.1 Publication
Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine.1 Publication

Cofactori

Magnesium.1 Publication
Thiamine pyrophosphate.1 Publication

Enzyme regulationi

Alpha-ketoglutarate dehydrogenase and decarboxylase activities are inhibited by unphosphorylated GarA, and allosterically activated by acetyl-CoA, the main substrate of the TCA cycle. Both the phosphoadenosine and acetyl moieties of acetyl-CoA are important for activation because neither CoA nor the synthetic compound S-(2-acetamidoethyl)-ethanethioate (which mimics the terminal acetyl-phosphopantetheine group of acetyl-CoA) has an activation effect.2 Publications

Kineticsi

  1. KM=0.54 mM for alpha-ketoglutarate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei314 – 3141Proton acceptor; for succinyltransferase activity By similarity
Binding sitei579 – 57912-oxoglutarate
Binding sitei604 – 60412-oxoglutarate
Metal bindingi645 – 6451Magnesium
Metal bindingi678 – 6781Magnesium
Metal bindingi680 – 6801Magnesium; via carbonyl oxygen
Binding sitei952 – 9521Thiamine pyrophosphate
Binding sitei1020 – 102012-oxoglutarate
Binding sitei1038 – 10381Allosteric activator
Binding sitei1054 – 10541Allosteric activator
Binding sitei1142 – 11421Allosteric activator

GO - Molecular functioni

  1. 2-hydroxy-3-oxoadipate synthase activity Source: UniProtKB-EC
  2. 2-oxoglutarate decarboxylase activity Source: UniProtKB-EC
  3. dihydrolipoyllysine-residue succinyltransferase activity Source: UniProtKB-EC
  4. metal ion binding Source: UniProtKB-KW
  5. oxoglutarate dehydrogenase (succinyl-transferring) activity Source: UniProtKB-EC
  6. thiamine pyrophosphate binding Source: InterPro

GO - Biological processi

  1. tricarboxylic acid cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Decarboxylase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-5048-MONOMER.
UniPathwayiUPA00223; UER00997.
UPA00223; UER01001.

Names & Taxonomyi

Protein namesi
Recommended name:
Multifunctional 2-oxoglutarate metabolism enzyme
Alternative name(s):
2-hydroxy-3-oxoadipate synthase (EC:2.2.1.5)
Short name:
HOA synthase
Short name:
HOAS
2-oxoglutarate carboxy-lyase
2-oxoglutarate decarboxylase
Alpha-ketoglutarate decarboxylase (EC:4.1.1.71)
Short name:
KG decarboxylase
Short name:
KGD
Alpha-ketoglutarate-glyoxylate carboligase
Including the following 2 domains:
2-oxoglutarate dehydrogenase E1 component (EC:1.2.4.2)
Short name:
ODH E1 component
Alternative name(s):
Alpha-ketoglutarate dehydrogenase E1 component
Short name:
KDH E1 component
Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC:2.3.1.61)
Alternative name(s):
2-oxoglutarate dehydrogenase complex E2 component
Short name:
ODH E2 component
Short name:
OGDC-E2
Dihydrolipoamide succinyltransferase
Gene namesi
Name:kgd
Synonyms:sucA
Ordered Locus Names:MSMEG_5049, MSMEI_4922
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene do not show any ODH activity, in contrast to wild-type, demonstrating that this protein is part of a functional ODH complex in mycobacteria.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi539 – 5391H → A: Loss of KG decarboxylase activity. 1 Publication
Mutagenesisi579 – 5791H → A: Loss of KG decarboxylase activity. 1 Publication
Mutagenesisi747 – 7471H → A: 40-fold decrease in KG decarboxylase activity. 1 Publication
Mutagenesisi781 – 7811R → A: Increase in KG decarboxylase activity. 1 Publication
Mutagenesisi1020 – 10201H → A: Loss of KG decarboxylase activity. 1 Publication
Mutagenesisi1034 – 10341E → A: Loss of activation by acetyl-CoA. 1 Publication
Mutagenesisi1062 – 10621R → A: Loss of activation by acetyl-CoA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12271227Multifunctional 2-oxoglutarate metabolism enzymePRO_0000310718Add
BLAST

Interactioni

Subunit structurei

Homodimer. Interacts with the FHA domain of unphosphorylated GarA. The 2-oxoglutarate dehydrogenase (ODH) complex contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).2 Publications

Protein-protein interaction databases

IntActiA0R2B1. 1 interaction.
STRINGi246196.MSMEG_5049.

Structurei

Secondary structure

1
1227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi124 – 1329
Helixi134 – 14916
Helixi157 – 17115
Helixi173 – 1764
Beta strandi178 – 18912
Beta strandi196 – 1994
Beta strandi213 – 2164
Helixi219 – 2213
Helixi224 – 23815
Turni239 – 2413
Helixi245 – 2473
Beta strandi252 – 2565
Beta strandi275 – 2806
Helixi294 – 3007
Beta strandi305 – 3139
Turni314 – 3163
Helixi319 – 33214
Helixi336 – 34510
Helixi367 – 38014
Helixi381 – 3833
Helixi395 – 3984
Turni401 – 4033
Helixi406 – 4083
Helixi412 – 4143
Beta strandi416 – 4194
Beta strandi429 – 4313
Helixi432 – 44312
Beta strandi444 – 4507
Helixi457 – 46711
Helixi476 – 49924
Beta strandi500 – 5023
Helixi504 – 5063
Helixi514 – 52714
Beta strandi531 – 5366
Helixi542 – 5487
Helixi554 – 5574
Turni558 – 5603
Helixi567 – 5704
Beta strandi571 – 5733
Helixi576 – 5783
Beta strandi582 – 5876
Beta strandi589 – 5924
Beta strandi594 – 5996
Turni606 – 6094
Helixi610 – 62415
Beta strandi630 – 6323
Beta strandi637 – 6448
Helixi645 – 6506
Helixi652 – 6587
Turni659 – 6624
Turni664 – 6663
Beta strandi672 – 6776
Helixi686 – 6894
Beta strandi691 – 6944
Helixi697 – 7026
Beta strandi706 – 7105
Helixi714 – 73118
Beta strandi735 – 7406
Helixi753 – 7553
Helixi758 – 7647
Helixi770 – 78011
Helixi786 – 81227
Helixi822 – 8243
Helixi837 – 84610
Turni858 – 8603
Helixi861 – 87313
Helixi878 – 89114
Beta strandi895 – 9006
Turni901 – 9055
Beta strandi913 – 9164
Turni918 – 9203
Helixi926 – 9316
Beta strandi942 – 9476
Helixi953 – 96513
Beta strandi969 – 9746
Helixi978 – 9847
Helixi985 – 9906
Turni991 – 9944
Helixi995 – 9995
Beta strandi1006 – 10105
Beta strandi1014 – 10163
Helixi1025 – 10317
Beta strandi1034 – 10363
Beta strandi1038 – 10403
Helixi1045 – 105713
Beta strandi1064 – 10685
Helixi1071 – 10744
Beta strandi1076 – 10783
Helixi1082 – 10865
Beta strandi1092 – 10943
Helixi1097 – 11004
Helixi1106 – 11083
Beta strandi1111 – 11155
Helixi1119 – 113012
Beta strandi1135 – 11406
Beta strandi1142 – 11454
Helixi1148 – 11569
Beta strandi1163 – 11719
Beta strandi1174 – 11763
Helixi1177 – 118711
Helixi1189 – 11924
Beta strandi1196 – 12005
Beta strandi1204 – 12074
Helixi1211 – 122515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XT6X-ray2.74A/B116-1227[»]
2XT9X-ray2.20A361-1227[»]
2XTAX-ray2.20A/B/C/D361-1227[»]
2Y0PX-ray2.40A/B/C/D361-1227[»]
2YICX-ray1.96A/B/C/D361-1227[»]
2YIDX-ray2.25A/B/C/D361-1227[»]
3ZHQX-ray2.50A/B/C/D361-1227[»]
3ZHRX-ray2.10A/B/C/D361-1227[»]
3ZHSX-ray2.10A/B/C/D361-1227[»]
3ZHTX-ray2.15A/B/C/D361-1227[»]
3ZHUX-ray2.30A/B/C/D361-1227[»]
3ZHVX-ray2.30A/B/C/D361-1227[»]
ProteinModelPortaliA0R2B1.

Miscellaneous databases

EvolutionaryTraceiA0R2B1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 41412-oxoglutarate dehydrogenase E1, N-terminal partAdd
BLAST
Regioni42 – 8847LinkerAdd
BLAST
Regioni89 – 335247Succinyltransferase E2Add
BLAST
Regioni336 – 12278922-oxoglutarate dehydrogenase E1, C-terminal partAdd
BLAST
Regioni539 – 5402Thiamine pyrophosphate binding
Regioni604 – 6063Thiamine pyrophosphate binding
Regioni645 – 6473Thiamine pyrophosphate binding
Regioni1089 – 10924Allosteric activator
Regioni1149 – 11502Allosteric activator

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili783 – 81432 Reviewed predictionAdd
BLAST

Domaini

Is a fusion protein with two major domains exhibiting structural features of an E1 and E2 protein, and a short sequence stretch of E1 localized at the N-terminus, which is connected by a linker region to the rest of the protein By similarity.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0508.
HOGENOMiHOG000259587.
KOiK01616.
OMAiQHAPNKE.
OrthoDBiEOG6V1M1F.

Family and domain databases

Gene3Di3.30.559.10. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR001078. 2-oxoacid_DH_actylTfrase.
IPR011603. 2oxoglutarate_DH_E1.
IPR023213. CAT-like_dom.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view]
PANTHERiPTHR23152. PTHR23152. 1 hit.
PfamiPF00198. 2-oxoacid_dh. 1 hit.
PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
TIGRFAMsiTIGR00239. 2oxo_dh_E1. 1 hit.

Sequencei

Sequence statusi: Complete.

A0R2B1-1 [UniParc]FASTAAdd to Basket

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MSSSPSPFGQ NEWLVEEMYR KFRDDPSSVD PSWHEFLVDY SPEPTTDSAS     50
NGRTTTAAPV TPPTPAPAPA PEPKAAPKPA AKTEAKPAKP AKSATPAKGD 100
ESQILRGAAA AVVKNMNASL EVPTATSVRA IPAKLMIDNR VVINNHLKRT 150
RGGKISFTHL LGYAIVQAVK KFPNMNRHFA VVDGKPTAIT PAHTNLGLAI 200
DLQGKDGNRS LVVAAIKRCE TMRFGQFIAA YEDIVRRARD GKLTAEDFSG 250
VTISLTNPGT LGTVHSVPRL MQGQGAIIGA GAMEYPAEFQ GASEERIADL 300
GIGKLITLTS TYDHRIIQGA ESGDFLRTIH QLLLDDDFFD EIFRELGIPY 350
EPVRWRTDNP DSIEDKNARV IELIAAYRNR GHLMADIDPL RLDNTRFRSH 400
PDLDVNSHGL TLWDLDREFK VDGFAGVQRK KLRDILSVLR DAYCRHVGVE 450
YTHILEPEQQ RWIQERVETK HDKPTVAEQK YILSKLNAAE AFETFLQTKY 500
VGQKRFSLEG AETVIPMMDA VIDQCAEHGL DEVVIAMPHR GRLNVLANIV 550
GKPYSQIFSE FEGNLNPSQA HGSGDVKYHL GATGTYIQMF GDNDIEVSLT 600
ANPSHLEAVD PVLEGLVRAK QDLLDTGEEG SDNRFSVVPL MLHGDAAFAG 650
QGVVAETLNL ALLRGYRTGG TIHIVVNNQI GFTTAPTDSR SSEYCTDVAK 700
MIGAPIFHVN GDDPEACAWV ARLAVDFRQA FKKDVVIDML CYRRRGHNEG 750
DDPSMTQPYM YDVIDTKRGS RKAYTEALIG RGDISMKEAE DALRDYQGQL 800
ERVFNEVREL EKHEIEPSES VEADQQIPSK LATAVDKAML QRIGDAHLAL 850
PEGFTVHPRV RPVLEKRREM AYEGRIDWAF AELLALGSLI AEGKLVRLSG 900
QDTQRGTFTQ RHAVIVDRKT GEEFTPLQLL ATNPDGTPTG GKFLVYNSAL 950
SEFAAVGFEY GYSVGNPDAM VLWEAQFGDF VNGAQSIIDE FISSGEAKWG 1000
QLSDVVLLLP HGHEGQGPDH TSGRIERFLQ LWAEGSMTIA MPSTPANYFH 1050
LLRRHGKDGI QRPLIVFTPK SMLRNKAAVS DIRDFTESKF RSVLEEPMYT 1100
DGEGDRNKVT RLLLTSGKIY YELAARKAKE NREDVAIVRI EQLAPLPRRR 1150
LAETLDRYPN VKEKFWVQEE PANQGAWPSF GLTLPEILPD HFTGLKRISR 1200
RAMSAPSSGS SKVHAVEQQE ILDTAFG 1227
Length:1,227
Mass (Da):135,944
Last modified:January 9, 2007 - v1
Checksum:i76C5BFFD1638A391
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000480 Genomic DNA. Translation: ABK74238.1.
CP001663 Genomic DNA. Translation: AFP41366.1.
RefSeqiWP_011730279.1. NC_018289.1.
YP_006569661.1. NC_018289.1.
YP_889299.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK74238; ABK74238; MSMEG_5049.
AFP41366; AFP41366; MSMEI_4922.
GeneIDi4535402.
KEGGimsg:MSMEI_4922.
msm:MSMEG_5049.
PATRICi18082397. VBIMycSme59918_4927.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000480 Genomic DNA. Translation: ABK74238.1 .
CP001663 Genomic DNA. Translation: AFP41366.1 .
RefSeqi WP_011730279.1. NC_018289.1.
YP_006569661.1. NC_018289.1.
YP_889299.1. NC_008596.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XT6 X-ray 2.74 A/B 116-1227 [» ]
2XT9 X-ray 2.20 A 361-1227 [» ]
2XTA X-ray 2.20 A/B/C/D 361-1227 [» ]
2Y0P X-ray 2.40 A/B/C/D 361-1227 [» ]
2YIC X-ray 1.96 A/B/C/D 361-1227 [» ]
2YID X-ray 2.25 A/B/C/D 361-1227 [» ]
3ZHQ X-ray 2.50 A/B/C/D 361-1227 [» ]
3ZHR X-ray 2.10 A/B/C/D 361-1227 [» ]
3ZHS X-ray 2.10 A/B/C/D 361-1227 [» ]
3ZHT X-ray 2.15 A/B/C/D 361-1227 [» ]
3ZHU X-ray 2.30 A/B/C/D 361-1227 [» ]
3ZHV X-ray 2.30 A/B/C/D 361-1227 [» ]
ProteinModelPortali A0R2B1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi A0R2B1. 1 interaction.
STRINGi 246196.MSMEG_5049.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK74238 ; ABK74238 ; MSMEG_5049 .
AFP41366 ; AFP41366 ; MSMEI_4922 .
GeneIDi 4535402.
KEGGi msg:MSMEI_4922.
msm:MSMEG_5049.
PATRICi 18082397. VBIMycSme59918_4927.

Phylogenomic databases

eggNOGi COG0508.
HOGENOMi HOG000259587.
KOi K01616.
OMAi QHAPNKE.
OrthoDBi EOG6V1M1F.

Enzyme and pathway databases

UniPathwayi UPA00223 ; UER00997 .
UPA00223 ; UER01001 .
BioCyci MSME246196:GJ4Y-5048-MONOMER.

Miscellaneous databases

EvolutionaryTracei A0R2B1.

Family and domain databases

Gene3Di 3.30.559.10. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR001078. 2-oxoacid_DH_actylTfrase.
IPR011603. 2oxoglutarate_DH_E1.
IPR023213. CAT-like_dom.
IPR001017. DH_E1.
IPR029061. THDP-binding.
IPR005475. Transketolase-like_Pyr-bd.
[Graphical view ]
PANTHERi PTHR23152. PTHR23152. 1 hit.
Pfami PF00198. 2-oxoacid_dh. 1 hit.
PF00676. E1_dh. 1 hit.
PF02779. Transket_pyr. 1 hit.
[Graphical view ]
PIRSFi PIRSF000157. Oxoglu_dh_E1. 1 hit.
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 2 hits.
TIGRFAMsi TIGR00239. 2oxo_dh_E1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: FUNCTION IN 2-OXOGLUTARATE DECARBOXYLATION, ENZYME REGULATION, KINETIC PARAMETERS, INTERACTION WITH GARA.
    Strain: ATCC 700084 / mc(2)155.
  5. "Functional plasticity and allosteric regulation of alpha-ketoglutarate decarboxylase in central mycobacterial metabolism."
    Wagner T., Bellinzoni M., Wehenkel A., O'Hare H.M., Alzari P.M.
    Chem. Biol. 18:1011-1020(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 116-1227 IN COMPLEXES WITH THIAMINE PYROPHOSPHATE; ACETYL-COA; ENAMINE-THDP REACTION INTERMEDIATE AND MAGNESIUM, FUNCTION AS A MULTIFUNCTIONAL ENZYME, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, PATHWAY, MUTAGENESIS OF HIS-539; HIS-579; HIS-747; ARG-781; HIS-1020; GLU-1034 AND ARG-1062, DISRUPTION PHENOTYPE.
    Strain: ATCC 700084 / mc(2)155.

Entry informationi

Entry nameiKGD_MYCS2
AccessioniPrimary (citable) accession number: A0R2B1
Secondary accession number(s): I7GDF5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: January 9, 2007
Last modified: September 3, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi