ID A0A1B1Q2F6_9CHLB Unreviewed; 508 AA.
AC A0A1B1Q2F6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028,
GN ECO:0000313|EMBL:ANT65035.1};
GN ORFNames=Ptc2401_01262 {ECO:0000313|EMBL:ANT65035.1};
OS Prosthecochloris sp. CIB 2401.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=1868325 {ECO:0000313|EMBL:ANT65035.1, ECO:0000313|Proteomes:UP000092496};
RN [1] {ECO:0000313|EMBL:ANT65035.1, ECO:0000313|Proteomes:UP000092496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB 2401 {ECO:0000313|EMBL:ANT65035.1,
RC ECO:0000313|Proteomes:UP000092496};
RA Nabhan S., Bunk B., Sproeer C., Bryant D.A., Overmann J.;
RT "Genome Sequence of Prosthecochloris phaeum CIB2401 of the phylum
RT Chlorobi.";
RL Submitted (JUL-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016432; ANT65035.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B1Q2F6; -.
DR STRING; 1868325.Ptc2401_01262; -.
DR KEGG; proc:Ptc2401_01262; -.
DR PATRIC; fig|1868325.3.peg.1235; -.
DR InParanoid; A0A1B1Q2F6; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000092496; 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-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:UP000092496}.
FT DOMAIN 14..246
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 266..453
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 344
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 448
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 508 AA; 55093 MW; 17CF2B5E0BB2C668 CRC64;
MCNDYENGLI VNNIAVFGTA SDVGKSVIAT ALCRIFRNAG VDVAPFKAQN MSNNSGVTPD
GLEIGRAQVA QAEAARVVPS ADMNPVLLKP NTDIGAQVVL QGRAVANRSA REYFGDTSRW
REAAFESLRR LDAKHEMLVL EGAGSCAEMN LYERDFVNFK SAREADAAVI LVADIDRGGV
FAQVVGTMAL LPEEDRARVA GVIVNRFRGD ASLFLDGIRI LEERSGVPVL GVVPYFRGFS
IAAEDAVPLQ SVVDPVGVPD SRKISIAVLY FPHISNFTDL SVFDHEERVE VHYLHRPRSL
DGYQALVLPG SKNVRGDLHW LTDKGWATRI AAFRETGGVV VGICGGYQML GRMVADQHGV
EGEPGEDEGL GLLDVETELL REKTLCNASG VTCSGGLAVH GYEIHMGETR LCEGVDPFLK
VDLRNNVEVS ALDGAKSVDG KVFGTYFHGV FDGAVFREWF LKSLDAGYVP AAEPYDREQA
YDLLADHVAE YLDMELLLSI AGHSEAVE
//
