ID A0A1I0XZ88_9CLOT Unreviewed; 506 AA.
AC A0A1I0XZ88;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=SAMN04488528_101090 {ECO:0000313|EMBL:SFB06204.1};
OS Clostridium frigidicarnis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84698 {ECO:0000313|EMBL:SFB06204.1, ECO:0000313|Proteomes:UP000198619};
RN [1] {ECO:0000313|EMBL:SFB06204.1, ECO:0000313|Proteomes:UP000198619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12271 {ECO:0000313|EMBL:SFB06204.1,
RC ECO:0000313|Proteomes:UP000198619};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOKI01000010; SFB06204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XZ88; -.
DR STRING; 84698.SAMN04488528_101090; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000198619; 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.
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:UP000198619}.
FT DOMAIN 4..225
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 249..447
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 328
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 442
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 506 AA; 56128 MW; B5BC899FDEA2265C CRC64;
MAKIMVQGTG SNVGKSILVA ALCRIFKQDG LSVCPYKSQN MALNSYITMD GKEMGRAQVL
QAYAAGIEPQ VYMNPILLKP SSDHNCQVIV NGEVYSNSSA KEYHNLKPKF SNMLKEEFEK
IEKQFDVIVM EGAGSPAEIN LRDRDIVNMG MAELVDAPVV IVGDIDKGGV FASLVGTMVL
FSDDERKRVK ATIINKFRGD IDILTPGIEM LEERTEVPNL GVVPHFRLQL EEEDGAVEEI
NTEIKNKIDV AVVMLPHISN FTDVDAIKAE EDISVRFITS LNEFKNPDLL VIPGSKNTIG
DLNYLRESGL EDKIKHYEKQ GGMVLGICGG YQMLGKTLDD PHNVESMSET TEGLGILDAH
TVFEKKKITT RVNAELLPYG AEKLSMDTIK DDLYGYEIHM GTTTYGEKGK PLFNITSRNG
EAGTWEDGAI NEKGNVMGTY IHGIFDGISF REALMNKLRI NKGLDLKKSG RYEALREGEL
DKLADIVRKS LDMNKIYDII GIKPKQ
//