SST_EMENI
ID SST_EMENI Reviewed; 517 AA.
AC Q5AT15; C8VET6; O13389;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Serine O-succinyltransferase {ECO:0000305};
DE Short=SST {ECO:0000303|PubMed:28581482};
DE EC=2.3.1.- {ECO:0000269|PubMed:28581482};
DE Flags: Precursor;
GN Name=cysA {ECO:0000303|PubMed:11021945}; ORFNames=AN8565;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=11021945; DOI=10.1099/00221287-146-10-2695;
RA Grynberg M., Topczewski J., Godzik A., Paszewski A.;
RT "The Aspergillus nidulans cysA gene encodes a novel type of serine O-
RT acetyltransferase which is homologous to homoserine O-acetyltransferases.";
RL Microbiology 146:2695-2703(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 11267 / DSM 820;
RX PubMed=28581482; DOI=10.1038/nchembio.2397;
RA Bastard K., Perret A., Mariage A., Bessonnet T., Pinet-Turpault A.,
RA Petit J.L., Darii E., Bazire P., Vergne-Vaxelaire C., Brewee C., Debard A.,
RA Pellouin V., Besnard-Gonnet M., Artiguenave F., Medigue C., Vallenet D.,
RA Danchin A., Zaparucha A., Weissenbach J., Salanoubat M., de Berardinis V.;
RT "Parallel evolution of non-homologous isofunctional enzymes in methionine
RT biosynthesis.";
RL Nat. Chem. Biol. 13:858-866(2017).
CC -!- FUNCTION: Transfers a succinyl group from succinyl-CoA to L-serine,
CC forming succinyl-L-serine. Has also weak serine acetyl transferase
CC activity and homoserine succinyl transferase activity.
CC {ECO:0000269|PubMed:28581482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine + succinyl-CoA = CoA + O-succinyl-L-serine;
CC Xref=Rhea:RHEA:52820, ChEBI:CHEBI:33384, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57292, ChEBI:CHEBI:136856;
CC Evidence={ECO:0000269|PubMed:28581482};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-serine: step 1/2. {ECO:0000305|PubMed:11021945,
CC ECO:0000305|PubMed:28581482}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q10341}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. MetX family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB84208.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF029885; AAB84208.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AACD01000157; EAA66990.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF80811.1; -; Genomic_DNA.
DR RefSeq; XP_681834.1; XM_676742.1.
DR AlphaFoldDB; Q5AT15; -.
DR SMR; Q5AT15; -.
DR STRING; 162425.CADANIAP00003059; -.
DR ESTHER; emeni-CYSC; Homoserine_transacetylase.
DR EnsemblFungi; CBF80811; CBF80811; ANIA_08565.
DR EnsemblFungi; EAA66990; EAA66990; AN8565.2.
DR GeneID; 2868684; -.
DR KEGG; ani:AN8565.2; -.
DR VEuPathDB; FungiDB:AN8565; -.
DR eggNOG; ENOG502QR3J; Eukaryota.
DR HOGENOM; CLU_028760_7_0_1; -.
DR InParanoid; Q5AT15; -.
DR OMA; NPQPGWW; -.
DR OrthoDB; 1090515at2759; -.
DR BRENDA; 2.3.1.30; 517.
DR UniPathway; UPA00136; UER00199.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0009001; F:serine O-acetyltransferase activity; IMP:AspGD.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
DR GO; GO:0006534; P:cysteine metabolic process; IMP:AspGD.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_00296; MetX_acyltransf; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR008220; HAT_MetX-like.
DR PANTHER; PTHR32268; PTHR32268; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000443; Homoser_Ac_trans; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01392; homoserO_Ac_trn; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Amino-acid biosynthesis; Cysteine biosynthesis;
KW Mitochondrion; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..517
FT /note="Serine O-succinyltransferase"
FT /id="PRO_0000436606"
FT DOMAIN 134..386
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT REGION 36..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..144
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000305|PubMed:28581482"
FT REGION 413..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 461
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT ACT_SITE 498
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 307
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P45131"
FT SITE 275
FT /note="Important for acyl-CoA specificity"
FT /evidence="ECO:0000305|PubMed:28581482"
SQ SEQUENCE 517 AA; 56426 MW; C1B20CAB08714CBB CRC64;
MSPLNGVARS FPRPFQAVTR RPFRVVQPAI ACPSNSRSFN HSRSLRSTGS QSPAPSPRDS
SNPALSFPCL DAQEAKSALL SARSLGSGPE PSYTAGHHER FHSDEPLLLD WGGLLPEFDI
AYETWGQLNE KKDNVILLHT GLSASSHAHS TEANPKPGWW EKFIGPGKTL DTDKYFVICT
NVLGGCYGST GPSTVDPSDG KKYATRFPIL TIEDMVRAQF RLLDHLGVRK LYASVGSSMG
GMQSLAAGVL FPERVGKIVS ISGCARSHPY SIAMRHTQRQ VLMMDPNWAR GFYYDSIPPH
SGMKLAREIA TVTYRSGPEW EKRFGRKRAD PSKQPALCPD FLIETYLDHA GEKFCLEYDA
NSLLYISKAM DLFDLGLTQQ LATKKQRAEA QAKISSGTNT VNDASCSLTL PEQPYQEQPS
ASTSAEQSAS ASETGSAPND LVAGLAPLKD HQVLVIGVAS DILFPAWQQR EIAETLIQAG
NKTVEHIELG NDVSLFGHDT FLLDVKNVGG AVRKFLD
