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Database: UniProt
Entry: A0A1H7LAR8_STRJI
LinkDB: A0A1H7LAR8_STRJI
Original site: A0A1H7LAR8_STRJI 
ID   A0A1H7LAR8_STRJI        Unreviewed;       499 AA.
AC   A0A1H7LAR8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SAMN05414137_104427 {ECO:0000313|EMBL:SEK95978.1};
OS   Streptacidiphilus jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptacidiphilus.
OX   NCBI_TaxID=235985 {ECO:0000313|EMBL:SEK95978.1, ECO:0000313|Proteomes:UP000183015};
RN   [1] {ECO:0000313|Proteomes:UP000183015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277
RC   / KCTC 19219 / NBRC 100920 / 33214
RC   {ECO:0000313|Proteomes:UP000183015};
RA   Varghese N.;
RL   Submitted (OCT-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|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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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DR   EMBL; FOAZ01000004; SEK95978.1; -; Genomic_DNA.
DR   RefSeq; WP_042441426.1; NZ_FOAZ01000004.1.
DR   AlphaFoldDB; A0A1H7LAR8; -.
DR   STRING; 235985.SAMN05414137_104427; -.
DR   eggNOG; COG1492; Bacteria.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000183015; 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.
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:UP000183015}.
FT   DOMAIN          6..230
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          259..429
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        338
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   499 AA;  52534 MW;  2E122655C4546E14 CRC64;
     MSGALLVAGT TSDAGKSVVT AGICRWLKRQ GVKVAPFKAQ NMSLNSFVTL DGAEIGRAQA
     MQAAAAGALP EAAMNPVLLK PGGDGRSQVV VLGKPVAEVG ALDYRDRKPA LLRIALDCLA
     DLRSRHDVVI CEGAGSPAEI NLRDRDIANM GLAVAADLPV VVVGDIDRGG VFASMFGTLA
     LLSAEDQAHI AGWLVNKFRG DARLLQPGLD MLLQVTHRPA LGVLPMLSGL WLDAEDSLDL
     AGVMARGTSG PPAGSDVLRV SVVRVPRLSN FTDIDALAQE PGVLVRWATR PEELADADLV
     VLPGTRATVA DLAWLRDQGL DRAVAEHAAR GLPVLGVCGG YQMLARTIDD PVESKRGEVD
     GLGLLPVRIA FAQEKTLARP VGEGYGEVVH GYEIHHGVAT VEGGEPWLDG CHAGSVWGTT
     WHGALENDGF RRAFLREVAA VTGRDFVPAP DTCFAAAREE RLDRLGDLIA EHADTDALWR
     LIEGGAPQGL PFVPPGAPS
//
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