ID   ASST_METAC              Reviewed;         500 AA.
AC   Q8TPT4;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=L-aspartate semialdehyde sulfurtransferase {ECO:0000305};
DE            EC=2.8.1.16 {ECO:0000305|PubMed:25938369};
GN   OrderedLocusNames=MA_1821 {ECO:0000312|EMBL:AAM05227.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION, AND MUTAGENESIS OF CYS-54 AND CYS-131.
RX   PubMed=25315403; DOI=10.1111/mmi.12832;
RA   Rauch B.J., Gustafson A., Perona J.J.;
RT   "Novel proteins for homocysteine biosynthesis in anaerobic
RT   microorganisms.";
RL   Mol. Microbiol. 94:1330-1342(2014).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=25938369; DOI=10.1021/acs.biochem.5b00118;
RA   Allen K.D., Miller D.V., Rauch B.J., Perona J.J., White R.H.;
RT   "Homocysteine is biosynthesized from aspartate semialdehyde and hydrogen
RT   sulfide in methanogenic archaea.";
RL   Biochemistry 54:3129-3132(2015).
RN   [4]
RP   FUNCTION, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=28165724; DOI=10.1021/acs.biochem.6b00931;
RA   Rauch B.J., Klimek J., David L., Perona J.J.;
RT   "Persulfide formation mediates cysteine and homocysteine biosynthesis in
RT   Methanosarcina acetivorans.";
RL   Biochemistry 56:1051-1061(2017).
CC   -!- FUNCTION: Required for O-acetylhomoserine sulfhydrylase (OAHS)-
CC       independent homocysteine (Hcy) biosynthesis (PubMed:25315403,
CC       PubMed:25938369). Together with MA_1822, catalyzes the condensation of
CC       sulfide with aspartate semialdehyde to generate homocysteine
CC       (Probable). Likely functions through persulfide intermediate
CC       (PubMed:28165724). {ECO:0000269|PubMed:25315403,
CC       ECO:0000269|PubMed:25938369, ECO:0000269|PubMed:28165724,
CC       ECO:0000305|PubMed:25938369}.
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:0000305|PubMed:25938369};
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000305|PubMed:25938369}.
CC   -!- SUBUNIT: Forms homodimers. May form a complex with MA_1822.
CC       {ECO:0000269|PubMed:28165724}.
CC   -!- SIMILARITY: Belongs to the L-aspartate semialdehyde sulfurtransferase
CC       family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM05227.1; -; Genomic_DNA.
DR   RefSeq; WP_011021823.1; NC_003552.1.
DR   AlphaFoldDB; Q8TPT4; -.
DR   SMR; Q8TPT4; -.
DR   STRING; 188937.MA_1821; -.
DR   EnsemblBacteria; AAM05227; AAM05227; MA_1821.
DR   GeneID; 1473710; -.
DR   KEGG; mac:MA_1821; -.
DR   HOGENOM; CLU_043239_0_0_2; -.
DR   InParanoid; Q8TPT4; -.
DR   OMA; WVRGCYF; -.
DR   OrthoDB; 8710at2157; -.
DR   PhylomeDB; Q8TPT4; -.
DR   BioCyc; MetaCyc:MON-20451; -.
DR   BRENDA; 2.8.1.16; 7224.
DR   Proteomes; UP000002487; 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   Amino-acid biosynthesis; CBS domain; Methionine biosynthesis;
KW   Reference proteome; Repeat; Transferase.
FT   CHAIN           1..500
FT                   /note="L-aspartate semialdehyde sulfurtransferase"
FT                   /id="PRO_0000449825"
FT   DOMAIN          384..441
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          446..500
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   ACT_SITE        131
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000269|PubMed:28165724"
FT   MUTAGEN         54
FT                   /note="C->A: Loss of activity. Cannot grow on sulfide-only
FT                   medium."
FT                   /evidence="ECO:0000269|PubMed:25315403"
FT   MUTAGEN         131
FT                   /note="C->A: Can grow on sulfide-only medium."
FT                   /evidence="ECO:0000269|PubMed:25315403"
SQ   SEQUENCE   500 AA;  54346 MW;  7C720AACBEE0A12F CRC64;
     MVEKSVHEIN KKIEDGSVNV VTAEEMVGIV ENLGVEGAAR EVDVVTTGTF GAMCSSGLML
     NLGHSEPPIK IQKLWFNNVE AYSGLAAVDA YLGAAQISDT RGIQYGGAHV IEDLLRGKEL
     DVHATSYGTD CYPRKVLDTR ITLDDLNEAV LLNPRNAYQK YAAATNSSKR ILNTYMGELL
     PNFGNVTYSG AGVLSPLSND PDYETIGMGT RIFMGGAQGY IIGNGTQHSP SSSFGTLMLK
     GNLKEMSSDY LRAASFAGYG TTLYMGIGIP IPILNEKIAA STAVRDEDIF TDILDYAVGS
     RDKPVIKQVN YAELRSGSIE LEGKNTPTSS LSSFKNARKI ANELKEWVKH GKFFVSMPVE
     KLSREGSAKS MKQTQAVPLV KDVMADFIVT IKKNQTVQDA AKKIWENSFN HLAVVSDTGE
     LVGILTAWDI SKAVAENIFD SVESVMTKKV LTCAPNEPVD LAARRLDRYG VSAMPVIDTQ
     RKVLGIITSD NISKLLARRY