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Database: UniProt
Entry: B2HIQ7_MYCMM
LinkDB: B2HIQ7_MYCMM
Original site: B2HIQ7_MYCMM 
ID   B2HIQ7_MYCMM            Unreviewed;       492 AA.
AC   B2HIQ7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Conserved hypothetical carboxylase {ECO:0000313|EMBL:ACC41814.1};
GN   OrderedLocusNames=MMAR_3388 {ECO:0000313|EMBL:ACC41814.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC41814.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC41814.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
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DR   EMBL; CP000854; ACC41814.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HIQ7; -.
DR   STRING; 216594.MMAR_3388; -.
DR   KEGG; mmi:MMAR_3388; -.
DR   eggNOG; COG0439; Bacteria.
DR   HOGENOM; CLU_027790_0_0_11; -.
DR   OrthoDB; 4632333at2; -.
DR   Proteomes; UP000001190; Chromosome.
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   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          145..347
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   492 AA;  55150 MW;  9830D7806DE402CB CRC64;
     MTAGNPEPKP PRVLNGLSDV RAFFHNNKLP LYFISPTPFN LLGIDRWVRN FFYLTYFDSF
     EGAHSRVFVP RRRDRRDFDG MGDVCNHLLR DPETLEFIAR RGPGGKACFV MLDGETQALA
     RQAGLEVIHP PAELRHRLGS KIVMTRLANE AGVPSVPHLI GRAGSYEELS TLAHDAGLGD
     DLVIEAAYGN AGSATFFVRG ERDWDQCAAD LVEQPEIKVM KRIRNVEVCI EGTVTRHGTV
     IGPAMTSLVG YPELTPSKGA WCGNDVWREV LPPAQTRAAR EMVRKLGDVL SREGYRGYFE
     VDLLHDLDAN ELYLGEVNPR LSGASPMTNL TTEAYADMPL FLFHLLEYMD VEYELDIEEI
     NTRWERGYGE DEVWGQLIMS ETSPELELFT STPRTGVWRL HHDGSVSFAR QGNDWATLLD
     ESEAFYMRVA APGDLRCEGA QLGVLVTRGH LQTDDYQLTE RCQRWVKGLK AHFASTPLTP
     AAPIVSRLVA RA
//
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