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Protein

2-oxoglutarate carboxylase large subunit

Gene

cfiA

Organism
Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + 2-oxoglutarate + HCO3- = ADP + phosphate + oxalosuccinate.1 Publication

Cofactori

Mg2+By similarity, Mn2+By similarity, Co2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351Divalent metal cationBy similarity
Binding sitei105 – 1051SubstrateBy similarity
Metal bindingi196 – 1961Divalent metal cation; via carbamate groupBy similarity
Metal bindingi227 – 2271Divalent metal cationBy similarity
Metal bindingi229 – 2291Divalent metal cationBy similarity
Binding sitei362 – 3621SubstrateBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Biotin, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoglutarate carboxylase large subunitImported (EC:6.4.1.7)
Alternative name(s):
2-oxoglutarate carboxylase alpha subunit1 Publication
Gene namesi
Name:cfiAImported
Ordered Locus Names:HTH_1392, Hydth_1382
OrganismiHydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)
Taxonomic identifieri608538 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeHydrogenobacter
Proteomesi
  • UP000002574 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 6526522-oxoglutarate carboxylase large subunitPRO_0000402797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei196 – 1961N6-carboxylysineBy similarity
Modified residuei609 – 6091N6-biotinyllysinePROSITE-ProRule annotationBy similarity

Post-translational modificationi

Biotinylated.1 Publication

Interactioni

Subunit structurei

Heterohexadecamer of 8 large subunits and 8 small subunits.2 Publications

Protein-protein interaction databases

STRINGi608538.HTH_1392.

Structurei

3D structure databases

ProteinModelPortaliD3DJ41.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 288263CarboxyltransferaseSequence analysisAdd
BLAST
Domaini563 – 64381Biotinyl-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 385Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 biotinyl-binding domain.PROSITE-ProRule annotation
Contains 1 carboxyltransferase domain.Sequence analysis

Phylogenomic databases

eggNOGiENOG4107QSA. Bacteria.
COG0511. LUCA.
COG5016. LUCA.
HOGENOMiHOG000231389.
KOiK20140.
OMAiPKTPQQM.
OrthoDBiPOG091H0184.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001882. Biotin_BS.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR009057. Homeodomain-like.
IPR000891. PYR_CT.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D3DJ41-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAVEIMEEI REKFKEFEKG GFRKKILITD LTPRDGQQCK LATRVRTDDL
60 70 80 90 100
LPLCEAMDKV GFYAVEVWGG ATYDVCLRYL KEDPWERLRR IKEVMPNTKL
110 120 130 140 150
QMLFRGQNIV GYRPKSDKLV YKFVERAIKN GITVFRVFDA LNDNRNIKTA
160 170 180 190 200
VKAIKELGGE AHAEISYTRS PIHTYQKWIE YALEIAEMGA DWLSFKDATG
210 220 230 240 250
IIMPFETYAI IKGIKEATGG KLPVLLHNHD MSGTAIVNHM MAVLAGVDML
260 270 280 290 300
DTVLSPLAFG SSHPATESVV AMLEGTPFDT GIDMKKLDEL AEIVKQIRKK
310 320 330 340 350
YKKYETEYAG VNAKVLIHKI PGGMISNMVA QLIEANALDK IEEALEEVPN
360 370 380 390 400
VERDLGHPPL LTPSSQIVGV QAVLNVISGE RYKVITKEVR DYVEGKYGKP
410 420 430 440 450
PGPISKELAE KILGPGKEPD FSIRAADLAD PNDWDKAYEE TKAILGREPT
460 470 480 490 500
DEEVLLYALF PMQAKDFFVA REKGELHPEP VDELVETTEV KAGVVPGAAP
510 520 530 540 550
VEFEIVYHGE KFKVKVEGVS AHQEPGKPRK YYIRVDGRLE EVQITPHVEA
560 570 580 590 600
IPKGGPTPTA VQAEEKGIPK ATQPGDATAP MPGRVVRVLV KEGDKVKEGQ
610 620 630 640 650
TVAIVEAMKM ENEIHAPISG VVEKVFVKPG DNVTPDDALL RIKHIEEEVS

YG
Length:652
Mass (Da):72,546
Last modified:March 23, 2010 - v1
Checksum:i8D6C35B018DF9921
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB246889 Genomic DNA. Translation: BAF34932.1.
AP011112 Genomic DNA. Translation: BAI69843.1.
CP002221 Genomic DNA. Translation: ADO45767.1.
RefSeqiWP_012964023.1. NC_017161.1.

Genome annotation databases

EnsemblBacteriaiADO45767; ADO45767; Hydth_1382.
BAI69843; BAI69843; HTH_1392.
KEGGihte:Hydth_1382.
hth:HTH_1392.
PATRICi32211729. VBIHydThe36152_1403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB246889 Genomic DNA. Translation: BAF34932.1.
AP011112 Genomic DNA. Translation: BAI69843.1.
CP002221 Genomic DNA. Translation: ADO45767.1.
RefSeqiWP_012964023.1. NC_017161.1.

3D structure databases

ProteinModelPortaliD3DJ41.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi608538.HTH_1392.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADO45767; ADO45767; Hydth_1382.
BAI69843; BAI69843; HTH_1392.
KEGGihte:Hydth_1382.
hth:HTH_1392.
PATRICi32211729. VBIHydThe36152_1403.

Phylogenomic databases

eggNOGiENOG4107QSA. Bacteria.
COG0511. LUCA.
COG5016. LUCA.
HOGENOMiHOG000231389.
KOiK20140.
OMAiPKTPQQM.
OrthoDBiPOG091H0184.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR001882. Biotin_BS.
IPR000089. Biotin_lipoyl.
IPR003379. Carboxylase_cons_dom.
IPR009057. Homeodomain-like.
IPR000891. PYR_CT.
IPR011053. Single_hybrid_motif.
[Graphical view]
PfamiPF00364. Biotin_lipoyl. 1 hit.
PF00682. HMGL-like. 1 hit.
PF02436. PYC_OADA. 1 hit.
[Graphical view]
SUPFAMiSSF51230. SSF51230. 1 hit.
PROSITEiPS00188. BIOTIN. 1 hit.
PS50968. BIOTINYL_LIPOYL. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei2OCL_HYDTT
AccessioniPrimary (citable) accession number: D3DJ41
Secondary accession number(s): Q05KD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2011
Last sequence update: March 23, 2010
Last modified: September 7, 2016
This is version 44 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.