ID A0A017H5D1_9FUSO Unreviewed; 496 AA.
AC A0A017H5D1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=C095_10910 {ECO:0000313|EMBL:KID48215.1};
OS Fusobacterium necrophorum subsp. funduliforme B35.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=1226633 {ECO:0000313|EMBL:KID48215.1, ECO:0000313|Proteomes:UP000031184};
RN [1] {ECO:0000313|EMBL:KID48215.1, ECO:0000313|Proteomes:UP000031184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B35 {ECO:0000313|EMBL:KID48215.1,
RC ECO:0000313|Proteomes:UP000031184};
RA Benahmed F.H., Rasmussen M., Harbottle H., Soppet D., Nagaraja T.G.,
RA Davidson M.;
RT "An opportunistic ruminal bacterium that causes liver abscesses in
RT cattle.";
RL Submitted (AUG-2013) 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: 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:KID48215.1}.
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DR EMBL; AUZI01000027; KID48215.1; -; Genomic_DNA.
DR RefSeq; WP_005953337.1; NZ_AOJP01000005.1.
DR AlphaFoldDB; A0A017H5D1; -.
DR GeneID; 75074815; -.
DR PATRIC; fig|1226633.4.peg.2213; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000031184; 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}.
FT DOMAIN 7..230
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 256..443
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 335
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 435
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 496 AA; 56177 MW; FEC147CC1CB77CBE CRC64;
MKTHNNLMIM GTASGVGKSA TVTALCRIFQ KDGYRVCPFK SQNMALNSYV TKDGKEMGRA
QAVQAEAIGL EPQAWMNPIL LKPSHDKKIQ IIIEGKSFGN LTGSEYHKYK QNLLPKLEEI
YHRIEENYDI SVIEGAGSPA EINMLEEDIS NFGMARIANA PVILVADIDR GGVFASIYGT
IMLLGEKDRR RVQGIIINKF RGNVEVLKPG LEKIKALTGV PVLGVLPYAD FNLEDEDSLS
EKYQSFKFSK HSNQIKISVI KLKHISNATD MDALSMYEDV EIQFVTERSQ IGKEDMIIIP
GSKNTIDDLK WLKESGIAAE IMKRAKTETI IFGICGGFQM LGKKVKDPYH IEGEIEELDA
LGLFNLETIM EKEKTLVQYT GTLRVEKGML KALDNLELRG YEIHQGVTRG DEENLTDDDR
IVFVNKDNIM ATYLHGIFDN KEFTEALLNE IRRRKGLEEI NHNISYEEYK RKEFDKLEKL
VRENVDMDTI YKIMGL
//
