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Database: UniProt
Entry: E1IGE5_9CHLR
LinkDB: E1IGE5_9CHLR
Original site: E1IGE5_9CHLR 
ID   E1IGE5_9CHLR            Unreviewed;       485 AA.
AC   E1IGE5;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=OSCT_2396 {ECO:0000313|EMBL:EFO79711.1};
OS   Oscillochloris trichoides DG-6.
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Oscillochloridaceae; Oscillochloris.
OX   NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79711.1, ECO:0000313|Proteomes:UP000054010};
RN   [1] {ECO:0000313|EMBL:EFO79711.1, ECO:0000313|Proteomes:UP000054010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG-6 {ECO:0000313|EMBL:EFO79711.1,
RC   ECO:0000313|Proteomes:UP000054010};
RX   PubMed=21037015; DOI=10.1128/JB.00931-10;
RA   Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA   Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA   Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT   "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT   Oscillochloris trichoides subsp. DG-6.";
RL   J. Bacteriol. 193:321-322(2011).
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: 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:EFO79711.1}.
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DR   EMBL; ADVR01000106; EFO79711.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1IGE5; -.
DR   STRING; 765420.OSCT_2396; -.
DR   eggNOG; COG1492; Bacteria.
DR   HOGENOM; CLU_019250_2_2_0; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000054010; 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:UP000054010}.
FT   DOMAIN          1..230
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          248..438
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        323
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        431
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   485 AA;  51930 MW;  6FB9A0268CE3BDCD CRC64;
     MILGTASSVG KSTLVAALCR IAVRRGLRVA PFKAQNMSNN AGIAVGGGEV GRSTIVQAEA
     ARIRPTVQMN PVLIKPEGHR RSQIIVEGHP WRSMDALDYW QRKDALWEIV TRNLDALRSE
     YDLVIAEGAG SPVELNLKPR DIVNARVATY AQARTVLVGD IDAGGIFAQL LGTLMLLDPE
     ERALVVGLLV NRFRGDPALF TDGVSILEQR SGLPVLGVVP WITDLGLAEE DAVALERGPR
     TASGETVIAV IQLPAIANFD DFDPLAREPG VEVRYIERPD QLAGAAAVIL PGTKHTLAAR
     RWLRERGFDV ALSRFPGAIV GICGGYQLLG EAISDPLGVE GGGGAEAGLG LLPIETIFEH
     TKETVEVAAQ ATMPWAQGAP LRGYEIHAGR SHIRSAAGAP VAQITQRGDA ATNIADGCHT
     QDGRVWGCYI HGLFTSPAFR HAWLQQLGWQ PRSPNTNPLD PYERLADTVE EALGEEGVAR
     LLGVT
//
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