ASSTI_METJA
ID ASSTI_METJA Reviewed; 131 AA.
AC Q57563;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit {ECO:0000250|UniProtKB:Q8TPT3};
GN OrderedLocusNames=MJ0099;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
CC -!- FUNCTION: Required for O-acetylhomoserine sulfhydrylase (OAHS)-
CC independent homocysteine (Hcy) biosynthesis. Together with MJ0100,
CC catalyzes the condensation of sulfide with aspartate semialdehyde to
CC generate homocysteine. May be involved in the reduction of the
CC disulfide formed in MJ0100. {ECO:0000250|UniProtKB:Q8TPT3}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00711};
CC Note=Binds 2 [4Fe-4S] cluster. {ECO:0000255|PROSITE-ProRule:PRU00711};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000250|UniProtKB:Q8TPT3}.
CC -!- SUBUNIT: May form a complex with MJ0100.
CC {ECO:0000250|UniProtKB:Q8TPT3}.
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DR EMBL; L77117; AAB98079.1; -; Genomic_DNA.
DR PIR; C64312; C64312.
DR RefSeq; WP_010869591.1; NC_000909.1.
DR AlphaFoldDB; Q57563; -.
DR SMR; Q57563; -.
DR STRING; 243232.MJ_0099; -.
DR EnsemblBacteria; AAB98079; AAB98079; MJ_0099.
DR GeneID; 1450938; -.
DR KEGG; mja:MJ_0099; -.
DR eggNOG; arCOG02460; Archaea.
DR HOGENOM; CLU_152999_0_0_2; -.
DR InParanoid; Q57563; -.
DR OMA; TGVCPTE; -.
DR OrthoDB; 111853at2157; -.
DR PhylomeDB; Q57563; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProt.
DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR018449; NIL_domain.
DR Pfam; PF09383; NIL; 1.
DR SMART; SM00930; NIL; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Methionine biosynthesis; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..131
FT /note="L-aspartate semialdehyde sulfurtransferase iron-
FT sulfur subunit"
FT /id="PRO_0000159130"
FT DOMAIN 73..102
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 103..131
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 82
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 85
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 112
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 131 AA; 15105 MW; BDE45A4CD055B78E CRC64;
MRKRVYYWTD SEHINKPVIS DTILNTGVKI NILKAKVEPQ EAFLILELFG SKETIEKALN
YLSKFGEVEE ISKVIKRDLE KCVHCGCCIT QCPINVIYMD EDYNVVFKEE DCVGCKNCLK
ACPFKAIEIF E
