COBQ_DECAR
ID COBQ_DECAR Reviewed; 487 AA.
AC Q47JS8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Daro_0144;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(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}.
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DR EMBL; CP000089; AAZ44903.1; -; Genomic_DNA.
DR RefSeq; WP_011285913.1; NC_007298.1.
DR AlphaFoldDB; Q47JS8; -.
DR SMR; Q47JS8; -.
DR STRING; 159087.Daro_0144; -.
DR EnsemblBacteria; AAZ44903; AAZ44903; Daro_0144.
DR KEGG; dar:Daro_0144; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_4; -.
DR OMA; GREVHDP; -.
DR OrthoDB; 744477at2; -.
DR UniPathway; UPA00148; -.
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.
FT CHAIN 1..487
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332335"
FT DOMAIN 251..439
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 487 AA; 51874 MW; ABAA8F2550856FA2 CRC64;
MPCYSLMVQG TTSDAGKSTL VAALCRILKR RGVRVAPFKP QNMALNSAVT VDGGEIGRAQ
ALQALACGLA PHTDFNPVLL KPTTDKKAQV IIHGKVAIDL DAKAYHAYKP RAMGAVLESW
ARLTAEYECV VVEGAGSPAE INLRDRDIAN MGFAEAVDCP VIIVADIDRG GVFAHLVGTL
ELLSPSEKNR VKGFVINRFR GDIGLLESGL TWLEARTGKP VLGVLPYLHG LMLDAEDAIA
TAAVGGKKAA KLKVVAPAYP RVSNHNDLDP LRLHPEVDFR WIGPGETPPA ADLIVLPGSK
AVRADLDWLR AQGWDKAIHK HLRYGGKLIG LCGGYQMLGR MIHDPQGLEG QPGSTPGLGV
LAVETTLEAE KQLRNVSGHL SLPGRPAMTG YEIHLGVTRG EGLAKGAVEL ADGVHDGAIS
ADDQVFATYC HGVLDHPEAL TALLAWAGMS ESEQVDFAAR READLDRLAD SVEAALDWEK
LSALLPG
