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Database: UniProt
Entry: A0A1S1MP28_9GAMM
LinkDB: A0A1S1MP28_9GAMM
Original site: A0A1S1MP28_9GAMM 
ID   A0A1S1MP28_9GAMM        Unreviewed;       657 AA.
AC   A0A1S1MP28;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OHU90156.1};
GN   ORFNames=BET10_15415 {ECO:0000313|EMBL:OHU90156.1};
OS   Pseudoalteromonas amylolytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1859457 {ECO:0000313|EMBL:OHU90156.1, ECO:0000313|Proteomes:UP000179786};
RN   [1] {ECO:0000313|EMBL:OHU90156.1, ECO:0000313|Proteomes:UP000179786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JW1 {ECO:0000313|EMBL:OHU90156.1,
RC   ECO:0000313|Proteomes:UP000179786};
RA   Wu Y.-H., Cheng H., Jin X.-B., Wang C.-S., Xu X.-W.;
RT   "Pseudoalteromonas amylolytica sp. nov., isolated from the surface
RT   seawater.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OHU90156.1}.
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DR   EMBL; MKJU01000027; OHU90156.1; -; Genomic_DNA.
DR   RefSeq; WP_070986121.1; NZ_MKJU01000027.1.
DR   AlphaFoldDB; A0A1S1MP28; -.
DR   STRING; 1859457.BET10_15415; -.
DR   OrthoDB; 9802769at2; -.
DR   Proteomes; UP000179786; Unassembled WGS sequence.
DR   GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1901607; P:alpha-amino acid biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR   Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE   4: Predicted;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          91..141
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
FT   DOMAIN          214..643
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
SQ   SEQUENCE   657 AA;  72662 MW;  2BD75AA7F8397438 CRC64;
     MSKNYIDTNG RAFVLTNTPQ QIEVQINNQG VKSLDEYLKQ DICNDLLDNI STDEITPGWC
     CFWYDEKLAD FAYLGLRQGV VHEGDIKRIN PCVIVSGNSK GCGSSREHSP YAEKALGAKV
     IVAKSFEKIY YQNCINIGLF PTTDFSILEY VFDKQPIPLD KFSESMSRID REIIYKGGLF
     KFNIEHHKNK QPITVFDEAT PLNLLQKIVK NRLSSIYSDH QSNEVSFCHV DLRFSHEYVS
     PMCISLFESE LGHNATLTDP TSIVCFQDHL TFLEQTLPAQ KQHLAVQANR LIETQLEFVK
     LNGLTYYSGR SASEKSAICH NAVMEDLALP GQVIIGTDSH TCTAGALGCF AFGVGATDMA
     NAWFTKDVKF TMPKTVAIEL VGELPPWCTA KDIVLQLLTL DFFKHSEALG CVLLYKGDGI
     KHLSIDERAT IANMAVEMGA TTAIFEVDSV TLDYIEKMRD LPEHQVTALL ELVNDDDAQF
     DHQLSLELSS VSPSIALPGD PRNVHSLEHI LAQRLNTITV DRAYAGSCTG GKNSDMDLYA
     QVLLHAKKLG LEKPDNIDFY IQFGSDNVKS YCEEKNYISL FESFGAKLID PSCGACINAG
     PGVSKQSSEV TISSQNRNFP GRSGPGSVYL ASPTVVAIAA VAGKLMTPSE FFSKNEH
//
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