ID A0A1Q9K206_9FIRM Unreviewed; 669 AA.
AC A0A1Q9K206;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=BHF69_08145 {ECO:0000313|EMBL:OLR62649.1};
OS Anaerostipes sp. 992a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR62649.1, ECO:0000313|Proteomes:UP000187371};
RN [1] {ECO:0000313|EMBL:OLR62649.1, ECO:0000313|Proteomes:UP000187371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=992a {ECO:0000313|EMBL:OLR62649.1,
RC ECO:0000313|Proteomes:UP000187371};
RX PubMed=27613689;
RA Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT Transferases and Their Diversity in the Proximal Colon of Swine.";
RL Appl. Environ. Microbiol. 82:6788-6798(2016).
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:OLR62649.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJIG01000004; OLR62649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9K206; -.
DR STRING; 1261637.BHF69_08145; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000187371; Unassembled WGS sequence.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008817; F:corrinoid adenosyltransferase 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; 2.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR003724; CblAdoTrfase_CobA.
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; PF02572; CobA_CobO_BtuR; 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; 2.
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:UP000187371}.
FT DOMAIN 6..229
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 252..436
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 429
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 669 AA; 75787 MW; 118A90FFED00392D CRC64;
MKLRPLMIQG TMSNSGKTFV TAGLCRIFAR DGYRCAPFKS QNMALNSYIT RDGWEIGRAQ
AMQAEAAGIE PSVEMNPILL KPNSDMGSQV IVNGEVLGNY SASTYFQMKP KLKPAIEKAF
QQLEEQYDMV VLEGAGSPAE INLKEHDIVN MGMAQMADAN VILVADIDRG GVFASVYGTI
QLLEPEEQKR IKGIIINKFR GDVEILKPGL AMIEELTGIP VIGVLPYEKI QIDDEDSLSE
ELEHYEKGSG LDIAVIRLPH ISNFTDFGAL DMMEQVSLRY VTDKSQLGTP DVIILPGTKN
TMYDLKWLRE SGLEAMIWRQ RKESHIVGIC GGYQMMGEIL EDPDDVEHGG TIKGMGLLPL
KTVFSEQKTR TRKRAVLCKN PSVHAEGYEI HMGLTTPLEE GIETLFWLED GKKDGFITPD
RRIWGSYLHG VFDEESFRMD WLTPILEEKG IKNGKTAISH KEFKEMQYDK LEQLLRTHLD
MNKIYEIVKR NQEEKKRDPG CLHLYYGDGK GKTTAAMGLA IRAAGAGKQV LIYQFLKDNS
SSERKVLDTI PGITCIKGPD KVKFIRNMTQ EEKEENRRQN DQKLEDIIKI AGEYDVLILD
EALYAIGREQ LSEELLIRYL KERPWWQEVI LTGRDPSREM RALADYCTHI QKEKHPFDQG
LCSRKGIEY
//
