ID A0A1Y4HAU7_9FIRM Unreviewed; 492 AA.
AC A0A1Y4HAU7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=B5F36_07195 {ECO:0000313|EMBL:OUP03980.1};
OS Anaerofilum sp. An201.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerofilum.
OX NCBI_TaxID=1965588 {ECO:0000313|EMBL:OUP03980.1, ECO:0000313|Proteomes:UP000195817};
RN [1] {ECO:0000313|Proteomes:UP000195817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An201 {ECO:0000313|Proteomes:UP000195817};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00028}.
CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004953, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OUP03980.1}.
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DR EMBL; NFJT01000009; OUP03980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4HAU7; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000195817; Unassembled WGS sequence.
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-UniRule.
DR CDD; cd05389; CobQ_N; 1.
DR CDD; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047045; CobQ_N.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00313; cobQ; 1.
DR PANTHER; PTHR21343:SF1; COBYRIC ACID SYNTHASE; 1.
DR PANTHER; PTHR21343; DETHIOBIOTIN SYNTHETASE; 1.
DR Pfam; PF01656; CbiA; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis {ECO:0000256|ARBA:ARBA00022573, ECO:0000256|HAMAP-
KW Rule:MF_00028};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|HAMAP-Rule:MF_00028};
KW Reference proteome {ECO:0000313|Proteomes:UP000195817}.
FT DOMAIN 7..229
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 253..433
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 428
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 53240 MW; A0407EFAB22CD5D6 CRC64;
MKQAKCIMVQ GTMSGAGKSL LCAGLCRVFA QNGLRVAPFK SQNMALNSYV TRDGLEMGRA
QVVQAQAAGK EPDVRMNPIL LKPSSDIGSQ VIVNGEIRGQ MSAAEYFKIK RQLIPDILKA
YNSLAAENDI IVIEGAGSPA EINLRSDDIV NMGMAELVDA PVLLAGDIDR GGVFAQLYGT
VALLEERERA RIGGLIVNKF RGDEAILRPG LAMLEEKTGI PVLGVVPYLQ VNVDDEDSLA
PCLENRGGKK PLDIAVVRLP RISNFTDFSL LDEHPAMGVR YVQSVRELGN PDLVILPGTK
STLSDLLWLR QSGLEAAVCK LAHTGTPVLG ICGGYQMLGE TLADPHGTEG GGEMHGMGLL
PIDTVFSDRK TRTRMQAKVL APDFAGAKLD GYEIHTGKTT VRGDAFCLLE NGQPDGCVSG
NVFGTYLHGL FDTGSLTQKL AEYLCRRKGI PCEQAAPLSH REYQEQQFDL LADGIRRALD
MQAIYALMER KR
//