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Database: UniProt
Entry: COBQ_ALIF1
LinkDB: COBQ_ALIF1
Original site: COBQ_ALIF1 
ID   COBQ_ALIF1              Reviewed;         495 AA.
AC   Q5E0T7;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 2.
DT   13-SEP-2023, entry version 110.
DE   RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=VF_A0289;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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:0000255|HAMAP-Rule:MF_00028}.
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00028}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW87359.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000021; AAW87359.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_047863633.1; NC_006841.2.
DR   RefSeq; YP_206247.1; NC_006841.2.
DR   AlphaFoldDB; Q5E0T7; -.
DR   SMR; Q5E0T7; -.
DR   STRING; 312309.VF_A0289; -.
DR   EnsemblBacteria; AAW87359; AAW87359; VF_A0289.
DR   KEGG; vfi:VF_A0289; -.
DR   PATRIC; fig|312309.11.peg.2893; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_6; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000000537; Chromosome II.
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-KW.
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; Glutamine amidotransferase; Reference proteome.
FT   CHAIN           1..495
FT                   /note="Cobyric acid synthase"
FT                   /id="PRO_0000141339"
FT   DOMAIN          249..442
FT                   /note="GATase cobBQ-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        330
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT   ACT_SITE        434
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   495 AA;  54245 MW;  4233CBD8468CC263 CRC64;
     MRKYSPLMVQ GTTSDAGKTV LVAGLCRLLA NKGIQVAPFK PQNMALNSAV TEDGGEIGRA
     QALQADAARV KPHVHMNPIL LKPNTDIGAQ VIVQGKAIET MDAWGFHDYK KLAMPYVLES
     FSYLSNNYEC VVIEGAGSPA EINLRENDIA NMGFAEAADV PVIIVADIDR GGVFAHLYGT
     LALLSESEQA RVKGFVINRF RGDISLLVPG LEWLEEKTGK PVLGVIPYLH GLNLEAEDAI
     KSEQLDKGKF IVKVPVVTRI SNHTDFDPLR LHPEIDLQFI GKGDSLSGAD FIILPGSKSV
     QADLEYIKSQ GWDKDIERHL RYGGKVMGIC GGYQMLGEHL ADPLGIEGVP CRVKGLGYLS
     ISTELQKQKQ LTLVEGTLAL PNQNAVKVKG YEIHAGVSTN LGKEHIPISI HTKDAMRYDG
     TINDENSIFG TYLHGVFDEP EAFEAILTWA GLEKCQAINM HDIQEEAIER IAKSMEDSLD
     LSLIWPDVFE KNKAY
//
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