COBQ_AGARV
ID COBQ_AGARV Reviewed; 501 AA.
AC C4ZBD8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=EUBREC_1926;
OS Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835
OS / VPI 0990) (Eubacterium rectale).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospiraceae incertae sedis.
OX NCBI_TaxID=515619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / LMG 30912 / VPI
RC 0990;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001107; ACR75670.1; -; Genomic_DNA.
DR RefSeq; WP_012742767.1; NC_012781.1.
DR AlphaFoldDB; C4ZBD8; -.
DR SMR; C4ZBD8; -.
DR STRING; 515619.EUBREC_1926; -.
DR EnsemblBacteria; ACR75670; ACR75670; EUBREC_1926.
DR KEGG; ere:EUBREC_1926; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000001477; 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..501
FT /note="Cobyric acid synthase"
FT /id="PRO_1000201967"
FT DOMAIN 248..443
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 501 AA; 55511 MW; 55999601727985F9 CRC64;
MAKVIMVQGT MSNSGKSFLV AGLCRIFRQD GYRVAPFKSQ NMALNSYITD EGLEMGRAQV
MQAEAAGIKP MVCMNPILLK PTNNTGSQVI VNGRVLKNMP AREYFAYKKT LIPDIKKAFK
KLEEYADIIV IEGAGSPAEI NLKENDIVNM GLAHMVDAPV LLVGDIDRGG VFAQLLGTLM
LLTDEEKNRV CGLIINKFRG DKTILDPGIQ MLEERGRVPV TGVVPYMDVQ LEDEDSLTER
FDKKTDGLID IAVIRYPRIS NFTDFNVFEQ MSEVTVRYVS TVNELRHPDI VFLPGSKNTM
GDLLWMRQNG LEAAVKKLSC EIPVFGICGG YQMLGASIAD PDGVEEGGYM RGMELLPIDT
VLKDSKTRLQ TSGEIAHVDG VLSRLSGCHF LGYEIHMGKS AYSTASDEQG ACADRKNELN
NVISDGRNVY GSYIHGIFDT AEAARVIVDY IADKKGIDVN DSAIVSYKSF KEKQYDRLAD
TLREYLDMDA VYGMLREAKY D