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Database: UniProt
Entry: A0A1M4YP75_9THEO
LinkDB: A0A1M4YP75_9THEO
Original site: A0A1M4YP75_9THEO 
ID   A0A1M4YP75_9THEO        Unreviewed;       519 AA.
AC   A0A1M4YP75;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN   Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN   ORFNames=SAMN02746089_01255 {ECO:0000313|EMBL:SHF07609.1};
OS   Caldanaerobius fijiensis DSM 17918.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobius.
OX   NCBI_TaxID=1121256 {ECO:0000313|EMBL:SHF07609.1, ECO:0000313|Proteomes:UP000184088};
RN   [1] {ECO:0000313|EMBL:SHF07609.1, ECO:0000313|Proteomes:UP000184088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17918 {ECO:0000313|EMBL:SHF07609.1,
RC   ECO:0000313|Proteomes:UP000184088};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQVH01000011; SHF07609.1; -; Genomic_DNA.
DR   RefSeq; WP_073342877.1; NZ_FQVH01000011.1.
DR   AlphaFoldDB; A0A1M4YP75; -.
DR   STRING; 1121256.SAMN02746089_01255; -.
DR   OrthoDB; 9808302at2; -.
DR   UniPathway; UPA00148; -.
DR   Proteomes; UP000184088; 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:UP000184088}.
FT   DOMAIN          5..227
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
FT   DOMAIN          264..463
FT                   /note="CobB/CobQ-like glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF07685"
FT   ACT_SITE        343
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT   ACT_SITE        455
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ   SEQUENCE   519 AA;  58095 MW;  4B7A43BB558ADCE7 CRC64;
     MAMKIMVQGT ASSVGKSLIV TALCRIFKQD GYKVAPFKSQ NMALNSYITD DGLEMGRAQV
     AQAEACGLKP DVRMNPILLK PTSDRKSQVI LMGKVYKTMS AVEYQKFKPE LANFVADVFH
     SLEKEYDIIV IEGAGSPAEI NLREGDIVNM GMAEIADAPV LLVGDIDKGG VFASLAGTML
     LLAESEKERV KGVIINKFRG DIEILKPGIV MLEEIIKRPV LGVVPYVNIK IDEEDGATER
     FYRKTTYRDI EYSSGKDSSG EVIDVAVLHL PHISNFTDFD PLENMEGVNV RYVNEGQPIG
     KTDLIIIPGT KNTIGDLYAL RRNGWEEEIV KHRERGGFVI GICGGYQMLG ELIEDPGKIE
     SDMTVSRGLG LLNVRTTIKE HKVTAQVKAE ICCDCEMYRS LNGINIEGYE IHMGDTRHDE
     GVKVFARIYR RLSRDVEIYD GAVSDDGRVL GTYIHGIFEN SEFTRAFINI IRQQKGLRPI
     EACWDYKVYK ENQYDALADV VRRSLDMSKL YEIMKESLR
//
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