COBQ_RHOCB
ID COBQ_RHOCB Reviewed; 481 AA.
AC D5AV13; O68093; Q52686;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Cobyric acid synthase;
GN Name=cobQ; OrderedLocusNames=RCAP_rcc02051;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9256491; DOI=10.1073/pnas.94.17.9384;
RA Vlcek C., Paces V., Maltsev N., Paces J., Haselkorn R., Fonstein M.;
RT "Sequence of a 189-kb segment of the chromosome of Rhodobacter capsulatus
RT SB1003.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9384-9388(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on
CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine,
CC and one molecule of ATP is hydrogenolyzed for each amidation (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000305}.
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DR EMBL; AF010496; AAC16180.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85795.1; -; Genomic_DNA.
DR PIR; T03527; T03527.
DR RefSeq; WP_013067774.1; NC_014034.1.
DR AlphaFoldDB; D5AV13; -.
DR STRING; 272942.RCAP_rcc02051; -.
DR EnsemblBacteria; ADE85795; ADE85795; RCAP_rcc02051.
DR GeneID; 31490913; -.
DR KEGG; rcp:RCAP_rcc02051; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_5; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase; Reference proteome.
FT CHAIN 1..481
FT /note="Cobyric acid synthase"
FT /id="PRO_0000409930"
FT DOMAIN 248..435
FT /note="GATase cobBQ-type"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 427
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 50138 MW; BE76D86D0C00DB5F CRC64;
MTALMIQGAG SNVGKSMLVA GLCRAARRRG LTVAPFKPQN MSNNAAVTAD GGEIGRAQAL
QALACGLEPV TDMNPILLKP ESDVGAQVVV QGKRLTTTRA RVYATLKPQL MGAVLESFNR
LKATHDLVIV EGAGSPAEVN LRAGDIANMG FARAADVPVV LVGDIDRGGV IAQIVGTQAV
LDPADAEMIS GFLINKFRGD VTLFDDGYRL IGARTGWRGF GTLPWFPLAH KLPAEDALDI
ASGPATGGTV IACLTLSRIA NFDDLDPLAA EPGVRMVMVQ PGQPIPAEAR LVILPGSKST
RGDLAFLREQ GWDIDLAAHV RRGGHVLGIC GGYQMLGRSV ADPEGIEGPA GTTPGLGLLD
VETVMTPDKR LTRVRATHAG SGLAVEGYEI HIGRTEGADR ARPFAIVEGQ NEGAMSADGR
VIGSYLHGLF GADAFRAAFL RGLGIRASGQ SHAAGVEAAL DALADHLETH LDVTGILALA
R