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Database: UniProt
Entry: A0A418YC14_9GAMM
LinkDB: A0A418YC14_9GAMM
Original site: A0A418YC14_9GAMM 
ID   A0A418YC14_9GAMM        Unreviewed;       462 AA.
AC   A0A418YC14;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=D1Z90_15470 {ECO:0000313|EMBL:RJG42029.1};
OS   Motilimonas pumila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadales genera incertae sedis; Motilimonas.
OX   NCBI_TaxID=2303987 {ECO:0000313|EMBL:RJG42029.1, ECO:0000313|Proteomes:UP000283255};
RN   [1] {ECO:0000313|EMBL:RJG42029.1, ECO:0000313|Proteomes:UP000283255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG42029.1,
RC   ECO:0000313|Proteomes:UP000283255};
RA   Wang F.;
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RJG42029.1, ECO:0000313|Proteomes:UP000283255}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PLHSC7-2 {ECO:0000313|EMBL:RJG42029.1,
RC   ECO:0000313|Proteomes:UP000283255};
RA   Wang F.-Q., Ren L.-H., Lin Y.-W., Sun G.-H., Du Z.-J., Zhao J.-X.,
RA   Liu X.-J., Liu L.-J.;
RT   "Motilimonas pumilus sp. nov., isolated from the gut of sea cucumber
RT   (Apostichopus japonicus).";
RL   Submitted (JAN-2019) 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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, 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:RJG42029.1}.
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DR   EMBL; QZCH01000022; RJG42029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418YC14; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000283255; 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.
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:UP000283255}.
FT   DOMAIN          5..226
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          250..422
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        416
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   462 AA;  50342 MW;  3F992FF85AB21388 CRC64;
     MAKPIMMLGC TSDAGKSLLA AAACRVLANR GIKVAPFKAQ NMSNNAAVTP DGLEIGRAQY
     LQAIAAKAVP DVRMNPVLLK PSADTFSQVI VNGKADPAIS AMPWMDRKSV LWQHVTTALH
     SLQQDYEQLV IEGAGSPAEI NLRAGDIVNM SVALETQADV YLISDIDRGG SFAHLLGTWA
     CLAPEEQALI KGFVLNKFRG DPALLGNAMD WLEQKTGIAT VANIPMYDHR LPEEDAFRGS
     DSFVKGELNV ALLIYPYAAN MDEFDPLFHQ QGINVSVIRE QQDLSKFDAV ILPGSKNSGA
     SMAYLKQTGL SQAIVEVASA GKLVLGICGG LQILGRQLKD PLHLEAGDFD GLGLLDIKTE
     LASVKATSQV QFQWQGGVMQ GYEIHHGQTH TTAKVSEFLQ TGNGWQQDNV LGIYLHGAFE
     NAVFMQWFAE RLGHDLHTQD WHHVIDQELD VLAEKFARDS WL
//
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