ID D9X6Q8_STRVT Unreviewed; 420 AA.
AC D9X6Q8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=SSQG_04493 {ECO:0000313|EMBL:EFL33975.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL33975.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG657757; EFL33975.1; -; Genomic_DNA.
DR RefSeq; WP_003992082.1; NZ_GG657757.1.
DR AlphaFoldDB; D9X6Q8; -.
DR STRING; 591159.SSQG_04493; -.
DR eggNOG; COG1181; Bacteria.
DR HOGENOM; CLU_029016_6_2_11; -.
DR OrthoDB; 24041at2; -.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000004184}.
FT DOMAIN 116..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 420 AA; 45027 MW; 10EE4CAAB0D2249F CRC64;
MRSHEYVLLL GADQYLRERA FSGAKQAADL PVWAAAEDPV RRPNRTFDHM LPADPKDPES
LLRAIRAHSA RGLHPRVVVP LNDWTLDAAN TVNRELGLGG LDATAVTNAR NKHAMKRALL
AGGVRTPRSA LVRSEPELLD AVEAIGLPVV IKPYDFGGSG GVVLATTREE AIAGLAESKA
VIAQYGAAFG ILGDKYLVER FVDSDDEVSV EVLCGAGRAQ VLAVTEKYLS PRPWFAELAH
LVPSHRTGDP VLTELAVQAC VALGIDRGLA HVEIKFDADG TPWVIEVAAR PGGDGIMDQV
ERAYSLNPYR LHVGSYLGQD LLDVVAAAVP VKTSAIAFLK AAPGRIEDVL DGKPLPPEVR
ALNISARPGD LSHAAKNWST REGLVELEWD QLFSAKTPLP VALAKELSDQ IFVTGEAAGE
//
