ID COBQ_DEHM1 Reviewed; 506 AA.
AC Q3Z7Y8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028}; OrderedLocusNames=DET0936;
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(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}.
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DR EMBL; CP000027; AAW39791.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3Z7Y8; -.
DR SMR; Q3Z7Y8; -.
DR STRING; 243164.DET0936; -.
DR KEGG; det:DET0936; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_0; -.
DR InParanoid; Q3Z7Y8; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000008289; Chromosome.
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.
FT CHAIN 1..506
FT /note="Cobyric acid synthase"
FT /id="PRO_0000332336"
FT DOMAIN 254..453
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 334
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 445
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 506 AA; 55255 MW; 520C102ABB1F8108 CRC64;
MNAMAKLIMV QGTSSNVGKS ILVTALCRIF KQDGYKVAPF KSQNMALNAF VTQEGGEIGR
AQAVQAEACG IAPSVDMNPI LMKPEADSKS QIVVNGKVDR TISAREYYEY APLLLDTALA
ALNRLREQND IVVIEGAGSP AEINLRQREI VNMRIAKTAG APVLLAGDID RGGVFASLIG
TIDLLEPEER SYVKGYLINK FRGDASLLKP AIDVLEDRTS IPVLGIIPYL RNMAIAQEDS
VYLDECKSGL GETDLDIAVI RLPRISNYDD FDALATDGAS VRFVSKTGEI GNPDLIIIPG
TKSTIPDMEY LWQNGLAETI IKKAGKGTHV LGVCGGYQIL GKMIYDPHKT ESETTELKGL
GLLDTETTFE KEKSTTQVSG QVRFNNGLLA DMAGCEVGGY EIHMGRTRLF TAQPAFQITK
TPKGPADYLD GASNAEGTVL GTYIHGIFES DSFRRGFLNA IRRYKGIPER QAGYFDRDKE
YDKLADIVRA SIDMNKIYDI LNEGIR
//
