COBQ_PHOV8
ID COBQ_PHOV8 Reviewed; 496 AA.
AC A6L4Y5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=BVU_3115;
OS Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 /
OS NBRC 14291 / NCTC 11154) (Bacteroides vulgatus).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Phocaeicola.
OX NCBI_TaxID=435590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC
RC 11154;
RX PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA Knight R.D., Gordon J.I.;
RT "Evolution of symbiotic bacteria in the distal human intestine.";
RL PLoS Biol. 5:1574-1586(2007).
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.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00028}.
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DR EMBL; CP000139; ABR40749.1; -; Genomic_DNA.
DR RefSeq; WP_012055547.1; NC_009614.1.
DR AlphaFoldDB; A6L4Y5; -.
DR SMR; A6L4Y5; -.
DR STRING; 435590.BVU_3115; -.
DR DNASU; 5304076; -.
DR EnsemblBacteria; ABR40749; ABR40749; BVU_3115.
DR KEGG; bvu:BVU_3115; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_10; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR BioCyc; BVUL435590:G1G59-3238-MON; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002861; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
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; PF01656; CbiA; 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..496
FT /note="Cobyric acid synthase"
FT /id="PRO_1000002347"
FT DOMAIN 256..444
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 337
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 55363 MW; 8D9D04A31053FE35 CRC64;
MKKNLHPIML AGTGSDVGKS VIAAALCRIF KQDGYRPAPF KAQNMALNSY ATPEGLEIGR
AQAVQAEAAG VPCHTDMNPL LLKPSSDHTS QVVLNGRPIG NRNAFEYFRK EGREELRQEV
NAAFDRLAAR YNPIVMEGAG SISEINLRDT DLVNMPMACY ADADVILVAD IDRGGVFASV
YGSVMLQTPE DKKRIKGVII NKFRGDIRLF ESGVKMMEDL CGIPVLGIIP YYRNIHIEEE
DSVGLDYKRM QAVEGKINIA VVLLRHLSNF TDFNRLERDE RVHLYYTNNT EDLAKADIIL
LPGSKSTLDD LYELRRNGVA QAVLRAHREG VTVMGICGGY QLMGLEIHDP EGVEGEIRQL
PGLGLLPVIT TMQGEKVTRQ VNFHFLENAE TCQGYEIHMG ETRPVPGEAV VPLNKLEDGG
EDGCFVNQKC MGSYIHGILD NQAFIDYLLE PYAEKLECHT VLDYRTYKEE QYDKLAEHVR
SHLNLPLLYQ IMSGND