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O26232

- PYRF_METTH

UniProt

O26232 - PYRF_METTH

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Protein

Orotidine 5'-phosphate decarboxylase

Gene

pyrF

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).

Catalytic activityi

Orotidine 5'-phosphate = UMP + CO2.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201Substrate
Binding sitei42 – 421Substrate
Active sitei72 – 721Proton donor
Binding sitei127 – 1271Substrate
Binding sitei202 – 2021Substrate; via amide nitrogen
Binding sitei203 – 2031Substrate

GO - Molecular functioni

  1. orotidine-5'-phosphate decarboxylase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: InterPro
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase

Keywords - Biological processi

Pyrimidine biosynthesis

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-129-MONOMER.
UniPathwayiUPA00070; UER00120.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotidine 5'-phosphate decarboxylase (EC:4.1.1.23)
Alternative name(s):
OMP decarboxylase
Short name:
OMPDCase
Short name:
OMPdecase
Gene namesi
Name:pyrF
Ordered Locus Names:MTH_129
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000005223: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228Orotidine 5'-phosphate decarboxylasePRO_0000134612Add
BLAST

Interactioni

Subunit structurei

Homodimer.4 Publications

Protein-protein interaction databases

STRINGi187420.MTH129.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi12 – 143Combined sources
Beta strandi15 – 195Combined sources
Helixi24 – 3411Combined sources
Helixi35 – 373Combined sources
Beta strandi39 – 446Combined sources
Helixi45 – 517Combined sources
Helixi54 – 6310Combined sources
Beta strandi66 – 738Combined sources
Helixi77 – 8913Combined sources
Beta strandi93 – 997Combined sources
Helixi103 – 11614Combined sources
Beta strandi119 – 1235Combined sources
Helixi129 – 1324Combined sources
Helixi135 – 14915Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi158 – 1603Combined sources
Helixi161 – 17111Combined sources
Beta strandi173 – 1797Combined sources
Helixi189 – 1924Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2015Combined sources
Helixi203 – 2064Combined sources
Beta strandi208 – 2103Combined sources
Helixi211 – 22414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DV7X-ray1.80A2-228[»]
1DVJX-ray1.50A/B/C/D2-226[»]
1KLYX-ray1.50A1-228[»]
1KLZX-ray1.50A1-228[»]
1KM0X-ray1.70A/B/C/D1-226[»]
1KM1X-ray1.60A/B1-226[»]
1KM2X-ray1.50A1-226[»]
1KM3X-ray1.50A1-226[»]
1KM4X-ray1.50A1-226[»]
1KM5X-ray1.50A1-226[»]
1KM6X-ray1.50A1-226[»]
1LOLX-ray1.90A/B1-226[»]
1LOQX-ray1.50A1-228[»]
1LORX-ray1.60A1-228[»]
1LOSX-ray1.90A/B/C/D1-228[»]
1LP6X-ray1.90A/B1-226[»]
1X1ZX-ray1.45A/B1-228[»]
2E6YX-ray1.60A/B1-228[»]
2ZZ1X-ray1.57A/B1-228[»]
2ZZ2X-ray1.53A/B1-228[»]
2ZZ3X-ray1.80A/B1-228[»]
2ZZ4X-ray1.67A/B1-228[»]
2ZZ5X-ray1.56A/B1-228[»]
2ZZ6X-ray1.66A/B1-228[»]
2ZZ7X-ray1.58A1-228[»]
3G18X-ray1.60A/B1-228[»]
3G1AX-ray1.50A/B1-228[»]
3G1DX-ray1.50A/B1-228[»]
3G1FX-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M1-228[»]
3G1HX-ray2.30A/B/C/D/E/F/G/H/I/J/K/L/M1-228[»]
3G1SX-ray1.40A/B1-228[»]
3G1VX-ray1.30A/B1-228[»]
3G1XX-ray1.55A/B1-228[»]
3G1YX-ray1.40A/B1-228[»]
3G22X-ray1.50A/B1-228[»]
3G24X-ray1.50A/B1-228[»]
3LHTX-ray1.35A/B1-228[»]
3LHUX-ray1.60A/B1-228[»]
3LHVX-ray1.35A/B/C/D1-228[»]
3LHWX-ray1.35A/B1-228[»]
3LHYX-ray1.40A/B1-228[»]
3LHZX-ray1.40A/B1-228[»]
3LI0X-ray1.50A/B1-228[»]
3LI1X-ray1.35A/B1-228[»]
3LLDX-ray1.45A/B1-228[»]
3LLFX-ray1.30A/B1-228[»]
3LTPX-ray1.40A/B1-228[»]
3LTSX-ray1.43A/B1-228[»]
3LTYX-ray1.50A/B1-228[»]
3LV5X-ray1.44A/B1-228[»]
3LV6X-ray1.45A/B1-228[»]
3M1ZX-ray1.42A/B1-228[»]
3M41X-ray1.40A/B1-228[»]
3M43X-ray1.30A/B1-228[»]
3M44X-ray1.40A/B1-228[»]
3M47X-ray1.20A/B1-228[»]
3M5XX-ray1.40A/B1-228[»]
3M5YX-ray1.46A/B1-228[»]
3M5ZX-ray1.35A/B1-228[»]
3NQ6X-ray1.49A/B1-228[»]
3NQ7X-ray1.44A/B1-228[»]
3NQAX-ray1.40A/B1-228[»]
3NQCX-ray1.53A/B1-228[»]
3NQDX-ray1.42A/B1-228[»]
3NQEX-ray1.42A/B1-228[»]
3NQFX-ray1.31A/B1-228[»]
3NQGX-ray1.42A/B1-228[»]
3NQMX-ray1.32A/B1-228[»]
3P5YX-ray1.60A/B1-228[»]
3P5ZX-ray1.30A/B1-228[»]
3P60X-ray1.40A/B1-228[»]
3P61X-ray1.40A/B1-228[»]
3PBUX-ray1.30A/B1-228[»]
3PBVX-ray1.30A/B1-228[»]
3PBWX-ray1.30A/B1-228[»]
3PBYX-ray1.30A/B1-228[»]
3PC0X-ray1.30A/B1-228[»]
3QEZX-ray1.54A/B1-228[»]
3QF0X-ray1.34A/B1-228[»]
3QMRX-ray1.32A/B1-228[»]
3QMSX-ray1.32A/B1-228[»]
3QMTX-ray1.32A/B1-228[»]
3RLUX-ray1.49A/B1-228[»]
3RLVX-ray1.42A/B1-228[»]
3SECX-ray1.70A1-226[»]
3SGUX-ray1.70A1-226[»]
3SIZX-ray1.32A/B1-228[»]
3SJ3X-ray1.26A/B1-228[»]
3SSJX-ray1.40A1-226[»]
3SW6X-ray1.50A1-226[»]
3SY5X-ray1.32A/B1-228[»]
3THQX-ray1.50A/B1-226[»]
3V1PX-ray1.37A/B1-228[»]
3W07X-ray1.03A1-228[»]
3WJWX-ray1.59A1-228[»]
3WJXX-ray1.23A1-228[»]
3WJYX-ray1.72A1-228[»]
3WJZX-ray1.39A1-228[»]
3WK0X-ray1.41A1-228[»]
3WK1X-ray1.60A1-228[»]
3WK2X-ray1.69A1-228[»]
3WK3X-ray1.26A1-228[»]
4FX6X-ray1.53M/N1-228[»]
4FX8X-ray1.94A/B1-228[»]
4FXRX-ray1.71A/B1-228[»]
4GC4X-ray1.42A/B1-228[»]
4LC6X-ray1.32A/B1-228[»]
4LC8X-ray1.32A/B1-228[»]
4LW7X-ray1.42A/B1-228[»]
4NT0X-ray1.77A/B1-228[»]
4NUWX-ray1.59A/B1-228[»]
4NX5X-ray1.59A/B1-228[»]
4O11X-ray1.59A/B1-228[»]
4O8RX-ray2.29A/B/C/D/E/F/G/H/I/J/K/L/M1-228[»]
ProteinModelPortaliO26232.
SMRiO26232. Positions 9-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO26232.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 7910Substrate binding
Regioni180 – 19011Substrate bindingAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0284.
KOiK01591.
OMAiTEMSHPG.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_01200_A. OMPdecase_type1_A.
InterProiIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamiPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTiSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01740. pyrF. 1 hit.
PROSITEiPS00156. OMPDECASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O26232-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRSRRVDVMD VMNRLILAMD LMNRDDALRV TGEVREYIDT VKIGYPLVLS
60 70 80 90 100
EGMDIIAEFR KRFGCRIIAD FKVADIPETN EKICRATFKA GADAIIVHGF
110 120 130 140 150
RGADSVRACL NVAEEMGREV FLLTEMSHPG AEMFIQGAAD EIARMGVDLG
160 170 180 190 200
VKNYVGPSTR PERLSRLREI IGQDSFLISP GVGAQGGDPG ETLRFADAII
210 220
VGRSIYLADN PAAAAAGIIE SIKDLLNP
Length:228
Mass (Da):24,915
Last modified:January 1, 1998 - v1
Checksum:iA7B65D94C8663D78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84635.1.
PIRiF69038.
RefSeqiNP_275272.1. NC_000916.1.
WP_010875768.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB84635; AAB84635; MTH_129.
GeneIDi1470090.
KEGGimth:MTH129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84635.1 .
PIRi F69038.
RefSeqi NP_275272.1. NC_000916.1.
WP_010875768.1. NC_000916.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DV7 X-ray 1.80 A 2-228 [» ]
1DVJ X-ray 1.50 A/B/C/D 2-226 [» ]
1KLY X-ray 1.50 A 1-228 [» ]
1KLZ X-ray 1.50 A 1-228 [» ]
1KM0 X-ray 1.70 A/B/C/D 1-226 [» ]
1KM1 X-ray 1.60 A/B 1-226 [» ]
1KM2 X-ray 1.50 A 1-226 [» ]
1KM3 X-ray 1.50 A 1-226 [» ]
1KM4 X-ray 1.50 A 1-226 [» ]
1KM5 X-ray 1.50 A 1-226 [» ]
1KM6 X-ray 1.50 A 1-226 [» ]
1LOL X-ray 1.90 A/B 1-226 [» ]
1LOQ X-ray 1.50 A 1-228 [» ]
1LOR X-ray 1.60 A 1-228 [» ]
1LOS X-ray 1.90 A/B/C/D 1-228 [» ]
1LP6 X-ray 1.90 A/B 1-226 [» ]
1X1Z X-ray 1.45 A/B 1-228 [» ]
2E6Y X-ray 1.60 A/B 1-228 [» ]
2ZZ1 X-ray 1.57 A/B 1-228 [» ]
2ZZ2 X-ray 1.53 A/B 1-228 [» ]
2ZZ3 X-ray 1.80 A/B 1-228 [» ]
2ZZ4 X-ray 1.67 A/B 1-228 [» ]
2ZZ5 X-ray 1.56 A/B 1-228 [» ]
2ZZ6 X-ray 1.66 A/B 1-228 [» ]
2ZZ7 X-ray 1.58 A 1-228 [» ]
3G18 X-ray 1.60 A/B 1-228 [» ]
3G1A X-ray 1.50 A/B 1-228 [» ]
3G1D X-ray 1.50 A/B 1-228 [» ]
3G1F X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L/M 1-228 [» ]
3G1H X-ray 2.30 A/B/C/D/E/F/G/H/I/J/K/L/M 1-228 [» ]
3G1S X-ray 1.40 A/B 1-228 [» ]
3G1V X-ray 1.30 A/B 1-228 [» ]
3G1X X-ray 1.55 A/B 1-228 [» ]
3G1Y X-ray 1.40 A/B 1-228 [» ]
3G22 X-ray 1.50 A/B 1-228 [» ]
3G24 X-ray 1.50 A/B 1-228 [» ]
3LHT X-ray 1.35 A/B 1-228 [» ]
3LHU X-ray 1.60 A/B 1-228 [» ]
3LHV X-ray 1.35 A/B/C/D 1-228 [» ]
3LHW X-ray 1.35 A/B 1-228 [» ]
3LHY X-ray 1.40 A/B 1-228 [» ]
3LHZ X-ray 1.40 A/B 1-228 [» ]
3LI0 X-ray 1.50 A/B 1-228 [» ]
3LI1 X-ray 1.35 A/B 1-228 [» ]
3LLD X-ray 1.45 A/B 1-228 [» ]
3LLF X-ray 1.30 A/B 1-228 [» ]
3LTP X-ray 1.40 A/B 1-228 [» ]
3LTS X-ray 1.43 A/B 1-228 [» ]
3LTY X-ray 1.50 A/B 1-228 [» ]
3LV5 X-ray 1.44 A/B 1-228 [» ]
3LV6 X-ray 1.45 A/B 1-228 [» ]
3M1Z X-ray 1.42 A/B 1-228 [» ]
3M41 X-ray 1.40 A/B 1-228 [» ]
3M43 X-ray 1.30 A/B 1-228 [» ]
3M44 X-ray 1.40 A/B 1-228 [» ]
3M47 X-ray 1.20 A/B 1-228 [» ]
3M5X X-ray 1.40 A/B 1-228 [» ]
3M5Y X-ray 1.46 A/B 1-228 [» ]
3M5Z X-ray 1.35 A/B 1-228 [» ]
3NQ6 X-ray 1.49 A/B 1-228 [» ]
3NQ7 X-ray 1.44 A/B 1-228 [» ]
3NQA X-ray 1.40 A/B 1-228 [» ]
3NQC X-ray 1.53 A/B 1-228 [» ]
3NQD X-ray 1.42 A/B 1-228 [» ]
3NQE X-ray 1.42 A/B 1-228 [» ]
3NQF X-ray 1.31 A/B 1-228 [» ]
3NQG X-ray 1.42 A/B 1-228 [» ]
3NQM X-ray 1.32 A/B 1-228 [» ]
3P5Y X-ray 1.60 A/B 1-228 [» ]
3P5Z X-ray 1.30 A/B 1-228 [» ]
3P60 X-ray 1.40 A/B 1-228 [» ]
3P61 X-ray 1.40 A/B 1-228 [» ]
3PBU X-ray 1.30 A/B 1-228 [» ]
3PBV X-ray 1.30 A/B 1-228 [» ]
3PBW X-ray 1.30 A/B 1-228 [» ]
3PBY X-ray 1.30 A/B 1-228 [» ]
3PC0 X-ray 1.30 A/B 1-228 [» ]
3QEZ X-ray 1.54 A/B 1-228 [» ]
3QF0 X-ray 1.34 A/B 1-228 [» ]
3QMR X-ray 1.32 A/B 1-228 [» ]
3QMS X-ray 1.32 A/B 1-228 [» ]
3QMT X-ray 1.32 A/B 1-228 [» ]
3RLU X-ray 1.49 A/B 1-228 [» ]
3RLV X-ray 1.42 A/B 1-228 [» ]
3SEC X-ray 1.70 A 1-226 [» ]
3SGU X-ray 1.70 A 1-226 [» ]
3SIZ X-ray 1.32 A/B 1-228 [» ]
3SJ3 X-ray 1.26 A/B 1-228 [» ]
3SSJ X-ray 1.40 A 1-226 [» ]
3SW6 X-ray 1.50 A 1-226 [» ]
3SY5 X-ray 1.32 A/B 1-228 [» ]
3THQ X-ray 1.50 A/B 1-226 [» ]
3V1P X-ray 1.37 A/B 1-228 [» ]
3W07 X-ray 1.03 A 1-228 [» ]
3WJW X-ray 1.59 A 1-228 [» ]
3WJX X-ray 1.23 A 1-228 [» ]
3WJY X-ray 1.72 A 1-228 [» ]
3WJZ X-ray 1.39 A 1-228 [» ]
3WK0 X-ray 1.41 A 1-228 [» ]
3WK1 X-ray 1.60 A 1-228 [» ]
3WK2 X-ray 1.69 A 1-228 [» ]
3WK3 X-ray 1.26 A 1-228 [» ]
4FX6 X-ray 1.53 M/N 1-228 [» ]
4FX8 X-ray 1.94 A/B 1-228 [» ]
4FXR X-ray 1.71 A/B 1-228 [» ]
4GC4 X-ray 1.42 A/B 1-228 [» ]
4LC6 X-ray 1.32 A/B 1-228 [» ]
4LC8 X-ray 1.32 A/B 1-228 [» ]
4LW7 X-ray 1.42 A/B 1-228 [» ]
4NT0 X-ray 1.77 A/B 1-228 [» ]
4NUW X-ray 1.59 A/B 1-228 [» ]
4NX5 X-ray 1.59 A/B 1-228 [» ]
4O11 X-ray 1.59 A/B 1-228 [» ]
4O8R X-ray 2.29 A/B/C/D/E/F/G/H/I/J/K/L/M 1-228 [» ]
ProteinModelPortali O26232.
SMRi O26232. Positions 9-228.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 187420.MTH129.

Chemistry

BindingDBi O26232.
ChEMBLi CHEMBL5688.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAB84635 ; AAB84635 ; MTH_129 .
GeneIDi 1470090.
KEGGi mth:MTH129.

Phylogenomic databases

eggNOGi COG0284.
KOi K01591.
OMAi TEMSHPG.

Enzyme and pathway databases

UniPathwayi UPA00070 ; UER00120 .
BioCyci MTHE187420:GJNM-129-MONOMER.

Miscellaneous databases

EvolutionaryTracei O26232.
PROi O26232.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
HAMAPi MF_01200_A. OMPdecase_type1_A.
InterProi IPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view ]
Pfami PF00215. OMPdecase. 1 hit.
[Graphical view ]
SMARTi SM00934. OMPdecase. 1 hit.
[Graphical view ]
SUPFAMi SSF51366. SSF51366. 1 hit.
TIGRFAMsi TIGR01740. pyrF. 1 hit.
PROSITEi PS00156. OMPDECASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  2. "Purification, crystallization and preliminary X-ray study of orotidine 5'-monophosphate decarboxylase."
    Wu N., Christendat D., Dharamsi A., Pai E.F.
    Acta Crystallogr. D 56:912-914(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  3. "Electrostatic stress in catalysis: structure and mechanism of the enzyme orotidine monophosphate decarboxylase."
    Wu N., Mo Y., Gao J., Pai E.F.
    Proc. Natl. Acad. Sci. U.S.A. 97:2017-2022(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEX WITH 6-AZAUMP, SUBUNIT.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  4. "Mapping the active site-ligand interactions of orotidine 5'-monophosphate decarboxylase by crystallography."
    Wu N., Gillon W., Pai E.F.
    Biochemistry 41:4002-4011(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF MUTANTS ALA-42; GLY-70; ALA-70; ALA-72; ALA-70/ALA-72; ASN-75; ALA-127 AND ALA-185 IN COMPLEX WITH DIFFERENT LIGANDS, SUBUNIT.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  5. "Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase."
    Wu N., Pai E.F.
    J. Biol. Chem. 277:28080-28087(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF COMPLEXES WITH BMP; CMP; UMP; XMP AND OF MUTANT DELTA ALA-203 IN COMPLEX WITH 6-AZAUMP, SUBUNIT.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF COMPLEX WITH BMP, SUBUNIT.
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiPYRF_METTH
AccessioniPrimary (citable) accession number: O26232
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: October 29, 2014
This is version 115 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, Complete proteome, 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