ID U7R2U4_PHOTE Unreviewed; 512 AA.
AC U7R2U4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|ARBA:ARBA00019833, ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=O185_06145 {ECO:0000313|EMBL:ERT13960.1};
OS Photorhabdus temperata J3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=1389415 {ECO:0000313|EMBL:ERT13960.1, ECO:0000313|Proteomes:UP000017133};
RN [1] {ECO:0000313|EMBL:ERT13960.1, ECO:0000313|Proteomes:UP000017133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J3 {ECO:0000313|EMBL:ERT13960.1,
RC ECO:0000313|Proteomes:UP000017133};
RA Park G.-S., Hong S.-J., Shin J.-H.;
RT "Whole Genome Shotgun Sequence of Photorhabdus temperata J3.";
RL Submitted (OCT-2013) 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|ARBA:ARBA00025166, 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|ARBA:ARBA00006205, ECO:0000256|HAMAP-Rule:MF_00028}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00605}.
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:ERT13960.1}.
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DR EMBL; AXDT01000048; ERT13960.1; -; Genomic_DNA.
DR RefSeq; WP_023044087.1; NZ_AXDT01000048.1.
DR AlphaFoldDB; U7R2U4; -.
DR PATRIC; fig|1389415.4.peg.1227; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000017133; 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.
DR PROSITE; PS51273; GATASE_TYPE_1; 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}.
FT DOMAIN 6..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 253..450
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 332
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 443
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 512 AA; 55852 MW; 870CFAACFA5C1790 CRC64;
MSLSLMLQGT ASDVGKSILV AGLCRIFVQD GYRCAPFKSQ NMALNSGITA NGEEMGRAQI
FQAEAAGIEP DVRMNPILLK PTSDCKAQVV LMGKVACSMN AVEYHQYKPH LQQQICEVFH
SLAREYDVMV LEGAGSPAEI NLRDRDIVNM GMAEMVDAPV LLVADIDRGG VFAAIYGTLA
LLLPEEKARI KGVIINKFRG DISLLQPGIE QIEALTGVPV LGVMPWLNID LEDEDGVALQ
TGKYDGAAEK ALDIAVVRLP YIANFTDFNA LAMQPDVRLR YVTQPSELQS SDLIILPGSK
NTLGDLRWLR QNGFVDALLT AHQSGIPVIG ICGGYQMLGK RIIDGVESGI DQMDGLGLLD
VETRFAHEKV TTRVNGSCLM ALPGLLSDCI EQPVRGYEIH MGSSLLGTDA TPFACITDRN
GQSGSWLDGA VNREGSVMGS YIHGLFDSTH FTRALLNALR QRKGLMAYQG DTLDYAHYKQ
TQFDLLAEAM REHLDIERIY QCMKSHQQGS AP
//
