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Database: UniProt
Entry: D3NV00_AZOS1
LinkDB: D3NV00_AZOS1
Original site: D3NV00_AZOS1 
ID   D3NV00_AZOS1            Unreviewed;       487 AA.
AC   D3NV00;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cbiP {ECO:0000313|EMBL:BAI72229.1};
GN   Synonyms=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN   ECO:0000313|EMBL:BAI72229.1};
GN   OrderedLocusNames=AZL_015910 {ECO:0000313|EMBL:BAI72229.1};
OS   Azospirillum sp. (strain B510).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI72229.1, ECO:0000313|Proteomes:UP000002040};
RN   [1] {ECO:0000313|EMBL:BAI72229.1, ECO:0000313|Proteomes:UP000002040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B510 {ECO:0000313|EMBL:BAI72229.1,
RC   ECO:0000313|Proteomes:UP000002040};
RX   PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA   Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA   Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA   Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA   Nakayama S., Yamada M., Tabata S., Sato S.;
RT   "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT   sp. B510.";
RL   DNA Res. 17:37-50(2010).
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}.
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DR   EMBL; AP010946; BAI72229.1; -; Genomic_DNA.
DR   RefSeq; WP_012974204.1; NC_013854.1.
DR   AlphaFoldDB; D3NV00; -.
DR   STRING; 137722.AZL_015910; -.
DR   KEGG; azl:AZL_015910; -.
DR   HOGENOM; CLU_019250_2_0_5; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000002040; Chromosome.
DR   GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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}; Ligase {ECO:0000313|EMBL:BAI72229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002040}.
FT   DOMAIN          6..238
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          254..438
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        334
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        432
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   487 AA;  51220 MW;  628C30767D3F7FF9 CRC64;
     MRSRAIMLQG TGSDVGKSLL VAGLCRALAR RGLTVRPFKP QNMSNNAAVT ADGGEIGRAQ
     ALQARACGVA PSVHMNPVLL KPQSDVGSQV VVRGVVVGTA RAADYQARKR ELLGTVLDSF
     ERLRAEADIV VVEGAGSPAE VNLRAGDIAN MGFATAADVP VLLVGDIDRG GVIASLVGTH
     ALLPKSEQEL IKGFLINKFR GDVRLFDEGL RIIERHTGWR GFGVVPWLKE AATLPAEDAV
     ALDRPRAAGE GALRVAVAML PHIANFDDFD PLAQEPGVAL TMVRPGRPLP GDADLVILPG
     TKTTIADLAF LRMQGWDIDL LAHWRRGGRV LGICGGYQML GRRIADPDGI EGPPGEAAGL
     GLLEVETVLM GPKVLEEAHG TERRTGAAVA GYEMHMGRTD GPDRARPMLE LAGGGTDGAE
     SADGRVAGCY LHGLFTADGF RAAYLRGLGG ALSDLDYGLA VERALDAVAE RLESVVDVEG
     LLRVAEG
//
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