ID   ASST_METJA              Reviewed;         509 AA.
AC   Q57564;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=L-aspartate semialdehyde sulfurtransferase {ECO:0000250|UniProtKB:Q8TPT4};
DE            EC=2.8.1.16 {ECO:0000250|UniProtKB:Q8TPT4};
GN   OrderedLocusNames=MJ0100;
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).
RN   [2]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=18931440; DOI=10.1107/s1744309108027930;
RA   Lucas M., Kortazar D., Astigarraga E., Fernandez J.A., Mato J.M.,
RA   Martinez-Chantar M.L., Martinez-Cruz L.A.;
RT   "Purification, crystallization and preliminary X-ray diffraction analysis
RT   of the CBS-domain pair from the Methanococcus jannaschii protein MJ0100.";
RL   Acta Crystallogr. F 64:936-941(2008).
RN   [3] {ECO:0007744|PDB:3KPB, ECO:0007744|PDB:3KPC, ECO:0007744|PDB:3KPD}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 388-509 IN COMPLEXES WITH
RP   S-ADENOSYL-L-METHIONINE AND S-METHYL-5'-THIOADENOSINE, ACTIVITY REGULATION,
RP   SUBUNIT, AND DOMAIN.
RX   PubMed=20026078; DOI=10.1016/j.jmb.2009.12.012;
RA   Lucas M., Encinar J.A., Arribas E.A., Oyenarte I., Garcia I.G.,
RA   Kortazar D., Fernandez J.A., Mato J.M., Martinez-Chantar M.L.,
RA   Martinez-Cruz L.A.;
RT   "Binding of S-methyl-5'-thioadenosine and S-adenosyl-L-methionine to
RT   protein MJ0100 triggers an open-to-closed conformational change in its CBS
RT   motif pair.";
RL   J. Mol. Biol. 396:800-820(2010).
CC   -!- FUNCTION: Required for O-acetylhomoserine sulfhydrylase (OAHS)-
CC       independent homocysteine (Hcy) biosynthesis. Together with MJ0099,
CC       catalyzes the condensation of sulfide with aspartate semialdehyde to
CC       generate homocysteine. Likely functions through persulfide
CC       intermediate. {ECO:0000250|UniProtKB:Q8TPT4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H(+) + hydrogen sulfide + L-aspartate 4-semialdehyde +
CC         reduced 2[4Fe-4S]-[ferredoxin] = H2O + L-homocysteine + oxidized
CC         2[4Fe-4S]-[ferredoxin]; Xref=Rhea:RHEA:58412, Rhea:RHEA-COMP:10002,
CC         Rhea:RHEA-COMP:10004, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29919, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC         ChEBI:CHEBI:58199, ChEBI:CHEBI:537519; EC=2.8.1.16;
CC         Evidence={ECO:0000250|UniProtKB:Q8TPT4};
CC   -!- ACTIVITY REGULATION: The ligand-induced conformational reorganization
CC       of the protein could be an important regulatory mechanism.
CC       {ECO:0000269|PubMed:20026078}.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000250|UniProtKB:Q8TPT4}.
CC   -!- SUBUNIT: Homodimer (PubMed:18931440, PubMed:20026078). May form a
CC       complex with MJ0099 (By similarity). {ECO:0000250|UniProtKB:Q8TPT4,
CC       ECO:0000269|PubMed:18931440, ECO:0000269|PubMed:20026078}.
CC   -!- DOMAIN: The C-terminal cystathionine beta-synthase (CBS) domains can
CC       bind different numbers of S-adenosyl-L-methionine (SAM) and S-methyl-
CC       5'-thioadenosine (MTA) ligands. Binding of SAM and MTA triggers a
CC       drastic conformational change in the protein, which evolves
CC       progressively from an open form in the absence of ligands to a closed
CC       form when the four sites are fully occupied.
CC       {ECO:0000269|PubMed:20026078}.
CC   -!- SIMILARITY: Belongs to the L-aspartate semialdehyde sulfurtransferase
CC       family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98080.1; -; Genomic_DNA.
DR   PIR; D64312; D64312.
DR   PDB; 3KPB; X-ray; 1.60 A; A/B/C/D=388-509.
DR   PDB; 3KPC; X-ray; 1.79 A; A=386-509.
DR   PDB; 3KPD; X-ray; 2.91 A; A/B/C/D=388-509.
DR   PDBsum; 3KPB; -.
DR   PDBsum; 3KPC; -.
DR   PDBsum; 3KPD; -.
DR   AlphaFoldDB; Q57564; -.
DR   SMR; Q57564; -.
DR   STRING; 243232.MJ_0100; -.
DR   EnsemblBacteria; AAB98080; AAB98080; MJ_0100.
DR   KEGG; mja:MJ_0100; -.
DR   eggNOG; arCOG00620; Archaea.
DR   HOGENOM; CLU_043239_0_0_2; -.
DR   InParanoid; Q57564; -.
DR   OMA; WVRGCYF; -.
DR   PhylomeDB; Q57564; -.
DR   BRENDA; 2.8.1.16; 3260.
DR   EvolutionaryTrace; Q57564; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002708; HcyBio.
DR   InterPro; IPR016426; MA1821-like.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01837; HcyBio; 1.
DR   PIRSF; PIRSF004698; UCP004698_CBS_MJ0100; 1.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; CBS domain; Methionine biosynthesis;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..509
FT                   /note="L-aspartate semialdehyde sulfurtransferase"
FT                   /id="PRO_0000106693"
FT   DOMAIN          394..450
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          455..509
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   ACT_SITE        133
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TPT4"
FT   BINDING         395
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         399
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         421
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         439
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         456
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         460
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         479..482
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   BINDING         497..500
FT                   /ligand="S-methyl-5'-thioadenosine"
FT                   /ligand_id="ChEBI:CHEBI:17509"
FT                   /evidence="ECO:0000269|PubMed:20026078"
FT   HELIX           390..393
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          394..397
FT                   /evidence="ECO:0007829|PDB:3KPD"
FT   HELIX           407..417
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          422..425
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          429..435
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   HELIX           437..445
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   HELIX           451..453
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          455..458
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   HELIX           468..478
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          481..486
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   STRAND          491..497
FT                   /evidence="ECO:0007829|PDB:3KPB"
FT   HELIX           498..505
FT                   /evidence="ECO:0007829|PDB:3KPB"
SQ   SEQUENCE   509 AA;  56458 MW;  81417970CD74F38F CRC64;
     MIMKTIKEIN EKIKKGEAVV VTAEEMIKIV EEEGAKRAAD YVDVVTTGTF GAMCSSGVFI
     NFGHSDPPIK MLRIYLNNVE AYGGLAAVDA YIGAAQPNED PDVDIDYGGA HVIEDLVRGK
     EVELYAEGYT TDCYPRKEVN VRITLDDVNQ AIMVNPRNCY QTYAAATNSR EEKIYTYMGI
     LLPEYNNVHY SGAGQLNPLQ NDYNPETKSF NTIGIGTRIF LGGGIGYVIG EGTQHNPPFG
     TLMVKGDLKQ MNPKFIRAAT MPRYGSTLYV GIGIPIPVLN EKIAERCAIR DEDIEVPIYD
     YGFPRRDRPL IAKTNYKVLR SGKITLNVNI DGKDVEKTVK TGSVSSYKMA REVAETLKQW
     ILDGKFLLTE RVDTLGRAEN KPMKSPITLV KDILSKPPIT AHSNISIMEA AKILIKHNIN
     HLPIVDEHGK LVGIITSWDI AKALAQNKKT IEEIMTRNVI TAHEDEPVDH VAIKMSKYNI
     SGVPVVDDYR RVVGIVTSED ISRLFGGKK