COBQ_DEHMB
ID COBQ_DEHMB Reviewed; 503 AA.
AC A5FQW8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cobyric acid synthase {ECO:0000255|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000255|HAMAP-Rule:MF_00028};
GN OrderedLocusNames=DehaBAV1_0820;
OS Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS BAV1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=216389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Ritalahti K.M., Loeffler F., Richardson P.;
RT "Complete sequence of Dehalococcoides sp. BAV1.";
RL Submitted (MAY-2007) 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: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; CP000688; ABQ17403.1; -; Genomic_DNA.
DR RefSeq; WP_011929119.1; NC_009455.1.
DR AlphaFoldDB; A5FQW8; -.
DR SMR; A5FQW8; -.
DR KEGG; deb:DehaBAV1_0820; -.
DR PATRIC; fig|216389.18.peg.869; -.
DR HOGENOM; CLU_019250_2_2_0; -.
DR OMA; EIHHGVA; -.
DR UniPathway; UPA00148; -.
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; cd01750; GATase1_CobQ; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_00028; CobQ; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR033949; CobQ_GATase1.
DR InterPro; IPR004459; CobQ_synth.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21343:SF1; PTHR21343:SF1; 1.
DR Pfam; PF07685; GATase_3; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00313; cobQ; 1.
DR PROSITE; PS51274; GATASE_COBBQ; 1.
PE 3: Inferred from homology;
KW Cobalamin biosynthesis; Glutamine amidotransferase.
FT CHAIN 1..503
FT /note="Cobyric acid synthase"
FT /id="PRO_1000074399"
FT DOMAIN 251..450
FT /note="GATase cobBQ-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
FT ACT_SITE 442
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00028"
SQ SEQUENCE 503 AA; 55038 MW; 5DAAFE18309C2496 CRC64;
MAKLIMVQGT SSNVGKSILV TALCRIFKQD GYKVAPYKSQ NMALNAFVTK EGGEIGRAQA
VQAEACGIEP SVDMNPILMK PEADSRSQII VNGKVDRTIS AREYYEYAPL LLDTALAALN
RLREKNDIVV IEGAGSPAEI NLKQREIVNM RIAKEASAPV LLAGDIDRGG VFASLIGTID
LLEPDERYYI KGYLINKFRG DASLLKPAID VLEDRTSIPV LGIIPYLRNM AIAQEDSVYL
DECKGNLGET DLDIAVIRLP RISNYDDFDA LATDGASVRF VSKTAEIGNP DLIIIPGTKS
TIPDMEYLEQ SGLAETIIKK ARKGTHVLGV CGGYQILGKM IYDPHKTESE TTELKGLGLL
DTETTFEKEK ATTQISGQVK FDSGLLSGLA GCAVSGYEIH MGRTRLFSAQ PAFHITKTPK
GPADYLDGAS NAEGTVLGTY IHGIFENAAF RRGFLNAIRR HKGIPERQAD YFDRDKEYDK
LADIVRASID MEKIYAILNE GIR
