ID G4FID7_9SYNE Unreviewed; 499 AA.
AC G4FID7;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=Syn8016DRAFT_0046 {ECO:0000313|EMBL:EHA63005.1};
OS Synechococcus sp. WH 8016.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=166318 {ECO:0000313|EMBL:EHA63005.1, ECO:0000313|Proteomes:UP000002752};
RN [1] {ECO:0000313|EMBL:EHA63005.1, ECO:0000313|Proteomes:UP000002752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH8016 {ECO:0000313|Proteomes:UP000002752};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Land M.L., Hauser L., Palenik B., Woyke T.J.;
RT "The draft genome of Synechococcus sp. WH 8016.";
RL Submitted (SEP-2011) 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:EHA63005.1}.
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DR EMBL; AGIK01000001; EHA63005.1; -; Genomic_DNA.
DR RefSeq; WP_006852186.1; NZ_AGIK01000001.1.
DR AlphaFoldDB; G4FID7; -.
DR STRING; 166318.Syn8016DRAFT_0046; -.
DR PATRIC; fig|166318.3.peg.51; -.
DR eggNOG; COG1492; Bacteria.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000002752; 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; 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; 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 1..228
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 250..443
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 329
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 499 AA; 54620 MW; FAC6933C9A067F77 CRC64;
MVLGTSSGAG KTLMTAALCR VLKRHGEQPL PFKGQNMSNN AWVDASGGEM AYSQAMQAWA
AKLEPCCAMN PVLLKPKGDS TSEVIHSGHS VGTARAEHYY RDWFRPGWKA IRSGLAELQQ
QWPDGRLVLE GAGSPVEVNL QKRDLTNLRL AQYLRANCLL VADIERGGVF AQIVGTLALL
RPVERPLVKG ILINRFRGRR ELFDEGRTWL EDHTGVPVLG VMPWLNDVFP PEDSLDLLER
KPTRGPTDLE IAVLKLPSLS NFSDLDPLET EPSVKLRWVA PGEDLGKPDA VVIPGSKQTL
RDLAAIHHSG LGDALCAYAF NGGHVFGICG GMQMLGETLG DPEGLEGGGS SQTNNHQGLG
LLPLHTLFSA DKALKQRSSV ARWPNGGSTL KLEGFELHHG RTTATETCQT LCLDAELGWV
NPIGEQGGLV AGTYLHGVFE SGPWRRRWLN QLRERKGLPP LREDQPHHSR QRDALLDRLA
DAFEQHIQLA PLLSNRPNG
//
