ID C3JD32_POREA Unreviewed; 499 AA.
AC C3JD32;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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:EEN81896.1};
GN ORFNames=POREN0001_0720 {ECO:0000313|EMBL:EEN81896.1};
OS Porphyromonas endodontalis (strain ATCC 35406 / BCRC 14492 / JCM 8526 /
OS NCTC 13058 / HG 370).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=553175 {ECO:0000313|EMBL:EEN81896.1, ECO:0000313|Proteomes:UP000004295};
RN [1] {ECO:0000313|EMBL:EEN81896.1, ECO:0000313|Proteomes:UP000004295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35406 / BCRC 14492 / JCM 8526 / NCTC 13058 / HG 370
RC {ECO:0000313|Proteomes:UP000004295};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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 -!- 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:EEN81896.1}.
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DR EMBL; ACNN01000036; EEN81896.1; -; Genomic_DNA.
DR RefSeq; WP_004335209.1; NZ_ACNN01000036.1.
DR AlphaFoldDB; C3JD32; -.
DR STRING; 553175.POREN0001_0720; -.
DR GeneID; 84818903; -.
DR eggNOG; COG1492; Bacteria.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000004295; Unassembled WGS sequence.
DR GO; GO:0015420; F:ABC-type vitamin B12 transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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}; Ligase {ECO:0000313|EMBL:EEN81896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004295}.
FT DOMAIN 10..238
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 260..445
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 439
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 499 AA; 55214 MW; 90625ACCF1226AD5 CRC64;
MKHPQPLRPI MLAGTGSDVG KSILATALCR IFKQDGYHPA PFKAQNMALN SYATPEGFEI
GRAQAVQAEA AGIPCHTDMN PLLLKPSSDQ TSQVVLHGKP IGNTHAYDYF RREGREELRA
EVHGAFDRLS SRFNPIVMEG AGSISELNLK DSDLVNMPMA RHAHAAVLLV ADIDRGGVFA
SVYGSIMLQS PEDRRLIKGV IINKFRGDLA LFTEGRKLLE ELTGVPVLGV VPYFQDITIE
EEDSVALTNK NRTSQVGKVN IAVVRTGHIS NFTDFSTLEQ DPRIHLYYTN NLKELEKADI
IILPGSKNTL GDLAELRNNG VAQCLVRAHR KGTTLVGICG GYQMMGQVLH DPDNLEGSGY
QHLPGLGLLP TETTITQEKV TRQVEFTHLG DPTLCRGYEI HMGQTTLLEG ASCSPTNQFS
DGTPEGTRLS ERCWGTYIHG ILDNPAVVDR LLAPFSHKLT QEKALDYASY KEEQYDKLAD
HVRQYVDVER IYQIMQDYD
//
