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Database: UniProt
Entry: A0A177MYK0_9GAMM
LinkDB: A0A177MYK0_9GAMM
Original site: A0A177MYK0_9GAMM 
ID   A0A177MYK0_9GAMM        Unreviewed;       505 AA.
AC   A0A177MYK0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=A1359_01755 {ECO:0000313|EMBL:OAI10788.1};
OS   Methylomonas lenta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=980561 {ECO:0000313|EMBL:OAI10788.1, ECO:0000313|Proteomes:UP000078476};
RN   [1] {ECO:0000313|EMBL:OAI10788.1, ECO:0000313|Proteomes:UP000078476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R-45370 {ECO:0000313|EMBL:OAI10788.1,
RC   ECO:0000313|Proteomes:UP000078476};
RA   Ploux O.;
RL   Submitted (MAR-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|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: 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:OAI10788.1}.
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DR   EMBL; LUUI01000149; OAI10788.1; -; Genomic_DNA.
DR   RefSeq; WP_066986547.1; NZ_LUUI01000149.1.
DR   AlphaFoldDB; A0A177MYK0; -.
DR   STRING; 980561.A1359_01755; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000078476; 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:UP000078476}.
FT   DOMAIN          6..232
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          253..433
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        332
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   505 AA;  54718 MW;  CFE62CC796178706 CRC64;
     MTPKALMVQG TTSDAGKSTL VTALCRHYHR QGVSVAPFKP QNMALNSAVT LDGGEIGRAQ
     AVQAAACGLP AHSDMNPVLL KPNTDTTAQV IIHGQVLQNQ SAVQYHDYKK VAKQAVLESW
     QRLTARYQTV IVEGAGSPAE INLRAGDIAN MGFAEAVDCP VILIADIDRG GVFAHIVGTL
     ALLSASEQQR VIGFVINRFR GDIALLQPGL DWLESETGKP VLAVLPYLHD LYLEAEDALC
     SRHAVSSSKT AFTIVVPHLP SFSNHTDFDP LQLHPGVQVV FAKSPEHIDG ADLVILPGSK
     SVRSDLARLK QQGWESFIHR HLRYGGKLLG ICGGFQMLGS AIHDPHGLEG EPGSAEGLNL
     LTFETTLQTH KRLRQMSGFF AHQSVPVAGY EIHMGISQGP ALNRPLFNLA SEDDGAISLD
     NQVAGSYLHG LFDVPAACDA LLNWAGYQQQ HAVDFNALRE SGIDRITDSW AEHCDFAKLD
     QALRQFYRQS DERTALSTAL NDFSS
//
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