ID A0A0A7EK81_9GAMM Unreviewed; 492 AA.
AC A0A0A7EK81;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=OM33_18330 {ECO:0000313|EMBL:AIY67034.1};
OS Pseudoalteromonas piratica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1348114 {ECO:0000313|EMBL:AIY67034.1, ECO:0000313|Proteomes:UP000030341};
RN [1] {ECO:0000313|EMBL:AIY67034.1, ECO:0000313|Proteomes:UP000030341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OCN003 {ECO:0000313|EMBL:AIY67034.1,
RC ECO:0000313|Proteomes:UP000030341};
RA Beurmann S., Videau P., Ushijima B., Smith A.M., Aeby G.S., Callahan S.M.,
RA Belcaid M.;
RT "Complete Genome Sequence of Pseudoalteromonas sp. Strain OCN003 Isolated
RT from Kaneohe Bay, Oahu, Hawaii.";
RL Submitted (NOV-2014) 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}.
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DR EMBL; CP009889; AIY67034.1; -; Genomic_DNA.
DR RefSeq; WP_040135757.1; NZ_CP009889.1.
DR AlphaFoldDB; A0A0A7EK81; -.
DR STRING; 1348114.OM33_18330; -.
DR KEGG; pseo:OM33_18330; -.
DR eggNOG; COG1492; Bacteria.
DR HOGENOM; CLU_019250_2_2_6; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000030341; Chromosome 2.
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:UP000030341}.
FT DOMAIN 7..236
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 253..437
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 430
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 492 AA; 54135 MW; DA699B53CDFC0974 CRC64;
MKAKQTLMVQ GTTSDAGKSV LVAALCRILS NHGYRVAPFK PQNMALNSAV TNDGGEIGRA
QAVQAEAARV EATVDMNPVL LKPNSDIGAQ VIVHGKSIGN SDAVDYHAMK PQLLGAVLES
HKRLSEAFEV VIVEGAGSPA EINLRDRDIA NMGFAEEADC PVVIVADIDK GGVFAHLVGT
YELLSETEKA RVKGFIINKF RGDITLLKPG NDWLEQKLGV PVLATIPFIP NLYIEPEDAL
DFNQIVTTQN ILNVTVVVYP RISNHTDFDV LRLHPNIKLH YARSPNQVNA CDLLILPGSK
SVMADLGYLI TEGWQTYINR HLRYGGKIFA ICGGMQMLGE KLYDPMCIES HQREVTGLGH
LPIQTTLMAN KTLNKTKGEC LETNTKVSGY EIHAGITEAL DECERIFKLE NGDFEGYQSS
DNQIKATYLH GIFDNPEYLT TILTWAGIEN MTSFDYEAEK DRQIEKLANA VECALPIEKI
ENLLSLPRNT AK
//
