ASSTI_METAC
ID ASSTI_METAC Reviewed; 130 AA.
AC Q8TPT3;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=L-aspartate semialdehyde sulfurtransferase iron-sulfur subunit {ECO:0000305};
GN OrderedLocusNames=MA_1822 {ECO:0000312|EMBL:AAM05228.1};
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.
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, 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 SUBUNIT.
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_1821, catalyzes the condensation of
CC sulfide with aspartate semialdehyde to generate homocysteine. May be
CC involved in the reduction of the disulfide formed in MA_1821
CC (Probable). {ECO:0000269|PubMed:25315403, ECO:0000269|PubMed:25938369,
CC ECO:0000305|PubMed:25938369}.
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:0000305|PubMed:25938369}.
CC -!- SUBUNIT: May form a complex with MA_1821.
CC {ECO:0000269|PubMed:28165724}.
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DR EMBL; AE010299; AAM05228.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TPT3; -.
DR STRING; 188937.MA_1822; -.
DR EnsemblBacteria; AAM05228; AAM05228; MA_1822.
DR KEGG; mac:MA_1822; -.
DR HOGENOM; CLU_152999_0_0_2; -.
DR InParanoid; Q8TPT3; -.
DR OMA; TGVCPTE; -.
DR PhylomeDB; Q8TPT3; -.
DR Proteomes; UP000002487; 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; PF12838; Fer4_7; 1.
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 1: Evidence at protein level;
KW 4Fe-4S; Amino-acid biosynthesis; Electron transport; Iron; Iron-sulfur;
KW Metal-binding; Methionine biosynthesis; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..130
FT /note="L-aspartate semialdehyde sulfurtransferase iron-
FT sulfur subunit"
FT /id="PRO_0000449826"
FT DOMAIN 72..101
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 102..130
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 81
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 121
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
SQ SEQUENCE 130 AA; 14467 MW; B6D46C898972E555 CRC64;
MSMKIKICIP TERIQNPIIS ETIVETGILL NIMVANIDST YGELIADVKD SRFARIKKAL
ESRGAIVAIL DRPIHRDEEE CVECGACISV CPMNVYSFDE TWSLCVDEKK CIQCGMCIKM
CPHGALKLGE
