ID A0A0P8Y9C9_9RHOB Unreviewed; 481 AA.
AC A0A0P8Y9C9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=JI58_08615 {ECO:0000313|EMBL:KPU83514.1};
OS Marinosulfonomonas sp. PRT-SC04.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marinosulfonomonas.
OX NCBI_TaxID=1527300 {ECO:0000313|EMBL:KPU83514.1, ECO:0000313|Proteomes:UP000054415};
RN [1] {ECO:0000313|EMBL:KPU83514.1, ECO:0000313|Proteomes:UP000054415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PRT-SC04 {ECO:0000313|EMBL:KPU83514.1};
RA Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT Rico Trench Inferred From Single Cell Genomes.";
RL Submitted (AUG-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}.
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:KPU83514.1}.
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DR EMBL; JPUR01000268; KPU83514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P8Y9C9; -.
DR PATRIC; fig|1527300.3.peg.1823; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000054415; 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.
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:UP000054415}.
FT DOMAIN 5..237
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 250..434
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 330
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 427
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 481 AA; 51070 MW; 37EDEE7521827622 CRC64;
MTKSLMIQGT GSNVGKSILV AGLARAYLRR GLTVRPFKPQ NMSNNAAVTC DGGEIGRAQA
LQARAAGVEP TTDMNPVLLK PESDIGAQVV VHGQRVATLK ARDYTAMKAS LMPAVLESFN
RLSRGVDLVL IEGAGSPAEI NLRAGDIANM GFAEAANVPV VLVGDIDRGG VIAQLVGTHV
VLAEPDRARI KGFIVNKFRG DVSLFDDGVT EIINRTGWTN IGVLPWFADA WRLPAEDVMD
IASTRGGNFK IAVPRLSRIA NFDDLDPLAA EPDVSVEIIE AGRPLPGDAD LILIPGSKST
IADLAYFREQ GWDIDLAAHV RRGGHVLGLC GGYQMLGKQI IDTDGIEGRA GSYQGLGLLD
VVTVMSPQKR LETSTAIYLP TGDPVRGYEI HIGNTEGPDC ARAWLDLGDR LDGAASADGR
VMGCYMHGLF TSDAFRASYL SGLGGTAGNA GYDDTVEATM DALADHLERH LDLDALLELA
E
//
