ID A0A1C5GWE2_9ACTN Unreviewed; 464 AA.
AC A0A1C5GWE2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cobyrinic acid a,c-diamide synthase {ECO:0000313|EMBL:SCG38126.1};
GN ORFNames=GA0070609_0526 {ECO:0000313|EMBL:SCG38126.1};
OS Micromonospora echinaurantiaca.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47857 {ECO:0000313|EMBL:SCG38126.1, ECO:0000313|Proteomes:UP000198217};
RN [1] {ECO:0000313|EMBL:SCG38126.1, ECO:0000313|Proteomes:UP000198217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43904 {ECO:0000313|EMBL:SCG38126.1,
RC ECO:0000313|Proteomes:UP000198217};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; LT607750; SCG38126.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5GWE2; -.
DR Proteomes; UP000198217; Chromosome i.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:InterPro.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004484; CbiA/CobB_synth.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR011698; GATase_3.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00379; cobB; 1.
DR PANTHER; PTHR43873; COBYRINATE A,C-DIAMIDE SYNTHASE; 1.
DR PANTHER; PTHR43873:SF1; COBYRINATE A,C-DIAMIDE SYNTHASE; 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 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW ECO:0000256|PROSITE-ProRule:PRU00606};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198217}.
FT DOMAIN 11..184
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT DOMAIN 273..421
FT /note="CobB/CobQ-like glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF07685"
FT REGION 234..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 47163 MW; D5C07D71CF9EDC94 CRC64;
MMTVVPRLVL SAPSSGHGKN ALAIGLLAAL ADRGDHVAGF KIGPDQVDAA YLGLAAGRPG
RNLDPRLVGA DRIAPLLGHG AAGAALALVQ GSMGLYDSLG GRPETESTAA VAIALRSPVV
LVVDVAAIGQ SVAALVHGFR SYDEQIWLGG VILNRVASAR HEALLREALD DIGVPVYGVL
RRQDLPPVLP ARRLGAVPAL AGSGEATRAV RRLGEAVAAT VDLDRLLGLA RSAPPLPAEP
WSPNPGGEPP AGERPVVALA GGPGGSYSHA ETAELLRAAG AEVVTVDPLR DEALPAGSRA
LVVGGGLPES YAEQLSANRR LCIAVAELAR TGRPVVAEGA GLLWLARELD GLPMCGVLDA
VGASREGLVV GYREATALTG TVVAPPGAVV AGHKAHRAVL TPRAGQRPVW SWSGGAPEGF
VWRGVHASQL VVHWAADPEI AARLVAAAAA EPAVEEARPG GVPA
//
