ID A0A401ILB3_APHSA Unreviewed; 495 AA.
AC A0A401ILB3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Cobyric acid synthase {ECO:0000256|HAMAP-Rule:MF_00028};
GN Name=cobQ {ECO:0000256|HAMAP-Rule:MF_00028};
GN ORFNames=AsFPU1_3463 {ECO:0000313|EMBL:GBF82039.1};
OS Aphanothece sacrum FPU1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Aphanothece.
OX NCBI_TaxID=1920663 {ECO:0000313|EMBL:GBF82039.1, ECO:0000313|Proteomes:UP000287247};
RN [1] {ECO:0000313|Proteomes:UP000287247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FPU1 {ECO:0000313|Proteomes:UP000287247};
RA Kanesaki Y., Yoshikawa S., Ohki K.;
RT "Physiological properties and genetic analysis related to exopolysaccharide
RT production of fresh-water unicellular cyanobacterium Aphanothece sacrum,
RT Suizenji Nori, that has been cultured as a food source in Japan.";
RL Submitted (MAY-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|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:GBF82039.1}.
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DR EMBL; BDQK01000014; GBF82039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ILB3; -.
DR OrthoDB; 9808302at2; -.
DR UniPathway; UPA00148; -.
DR Proteomes; UP000287247; 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:UP000287247}.
FT DOMAIN 4..230
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 252..443
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT ACT_SITE 331
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
FT ACT_SITE 436
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00028"
SQ SEQUENCE 495 AA; 54865 MW; 09A21F5EDE969D1D CRC64;
MKAIMVVGTT SHAGKSFLTA AICRILARQG WQVTPFKGQN MALNAYVTPS GGEIGYAQAV
QAWAAKIVPR VEMNPILLKP QGNMTSQVII KGKVIGTTKA SEYYENYFNL GWEAITSSLE
RLALEYDFVV CEGAGSPAEI NLKHRDLTNM RVACYLNAPT ILIVDIDRGG AFAHVVGTLQ
LLEPQERNLI KGIIINKFRG QRSLLDSGIE WLENYAGIPV LGVIPWRDII LPAEDSLDLL
ERRSRSSQSD INIVVMRLPH IANFTDFDPL DAEETVSLNY LNLNESLGYP DAVIIPGSKT
TIKDLMSLDK SGMAQQLQNY VAAGGVIFGI CGGFQMLGQT VFDPDQLEGD EVSYTALKML
PLDTIITSEK IVSQRQTNSH YPQAGLPIMG YEIHQGITRI SQSLSRFNVV KINPLFDDPN
LGYVNESKSI WGCYLHGVFD NGAWRRTWLN YLRNRRGLPS LPTGIANYRE QREANLDALA
DLVEEFVDLT PVLPK
//
