COBQ_DESHD
ID COBQ_DESHD Reviewed; 514 AA.
AC B8G242;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=Dhaf_1304;
OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=272564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10664 / DCB-2;
RX PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA Tiedje J.M.;
RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT anaerobe capable of dehalogenation and metal reduction.";
RL BMC Microbiol. 12:21-21(2012).
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; CP001336; ACL19360.1; -; Genomic_DNA.
DR RefSeq; WP_005812308.1; NC_011830.1.
DR AlphaFoldDB; B8G242; -.
DR SMR; B8G242; -.
DR EnsemblBacteria; ACL19360; ACL19360; Dhaf_1304.
DR KEGG; dhd:Dhaf_1304; -.
DR HOGENOM; CLU_019250_2_2_9; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000007726; 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.
FT CHAIN 1..514
FT /note="Cobyric acid synthase"
FT /id="PRO_1000116905"
FT DOMAIN 263..457
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 449
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 514 AA; 56682 MW; 66F498CF789DD675 CRC64;
MSGKKAAARL MIQGTSSNVG KSVLAAAFCR IFYQEGYHVA PFKAQNMALN SFITRSGGEM
GRAQVVQAQA AGLEPDVRMN PVLLKPTGHT GSQVIVLGKA QGTLSALKYH GDYQRKTWPI
VEEALHELLE EHEIVVIEGA GSPAEVNLKQ NDIVNMRVAK EAQAPVLLVA DIDRGGALAS
VVGTLELLEP EERQLVQGIV MNKFRGDIKL LQPALDFLEE RTGIPVVGVV PFYDQFKIPE
EDSVVLEEQN TSKRDQGKSR DEALDVAVIR LPYLSNFTDF DPFEDEPDVI LRYVREPSEL
GEPDCVIIPG SKNTLSDLRF LWESGLGEKI IKFWQEDVPI IGICGGYQML GRIVRDPLGT
ESDLKEIAGL GILPMETEFE LDKHTVQSRG KVVGGELFLA RCQGTEITGY EIHMGRSQGE
GHSLFEIEAQ ETAYGDGMSA GSAVGTYLHG IFDNDPLRTA LLEWLWERRG GTRPVGETMS
QAAIREQSFN ELADWVRNSM DMEKIRAMMG LHKG
