ID A0A1U9JLT5_9NEIS Unreviewed; 487 AA.
AC A0A1U9JLT5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=BXU06_08360 {ECO:0000313|EMBL:AQR65072.1};
OS Aquaspirillum sp. LM1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Aquaspirillum.
OX NCBI_TaxID=1938604 {ECO:0000313|EMBL:AQR65072.1, ECO:0000313|Proteomes:UP000188659};
RN [1] {ECO:0000313|EMBL:AQR65072.1, ECO:0000313|Proteomes:UP000188659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM1 {ECO:0000313|EMBL:AQR65072.1,
RC ECO:0000313|Proteomes:UP000188659};
RA Hentchel K., Vargas G., Fiebig A., Chen S.L., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (JAN-2017) 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 ---------------------------------------------------------------------------
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; CP019509; AQR65072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9JLT5; -.
DR STRING; 1938604.BXU06_08360; -.
DR KEGG; aql:BXU06_08360; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000188659; 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:UP000188659}.
FT DOMAIN 11..236
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 254..437
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 431
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 487 AA; 51997 MW; 7828AF6483B4000D CRC64;
MTPTDFPFSM LMVQGCTSDA GKSTLVAGLC RLLARDGVAV APFKPQNMAL NSAVTVDGGE
IGRAQALQAQ AAGLAAHSDF NPVLLKPSSD TGAQVIIHGR VRADMSARDY HHYKTTAMQA
VLESFARLRQ QYACVVVEGA GSPAEINLRA RDIANMGFAE AVDCPVILVA DIDRGGVFAH
LTGTLDCLSA SERARVVGFV INRFRGDIRL LQGGLDWLEA KTGKPVLAVL PYLHGLMLDA
EDAIQAEQRG EGLNVVVPVL PRISNHTDFD ALRAHPEVNL QFVGPDAPKP AADLVILPGS
KHTRADLAFL QAQGWPDYLR RHLRYGGKLI GICGGYQMLG QQIADPDGHE GQAGSSAGLG
LLAVNTTLAA SKQLRQVSGQ CSFANAPVSG YEIHLGHTDG ADCQRPAFVL DDGRTDGAIS
ADGQILGSYL HGLFDHPQAS QALLAWAGLH SQQQVDLNAL RETSLNRLAD ACLPLYQRLQ
QIDCRTR
//
