ID A1DG77_NEOFI Unreviewed; 534 AA.
AC A1DG77;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192, ECO:0000256|RuleBase:RU361204};
DE EC=4.2.1.22 {ECO:0000256|ARBA:ARBA00012041, ECO:0000256|RuleBase:RU361204};
GN ORFNames=NFIA_083350 {ECO:0000313|EMBL:EAW18384.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW18384.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC Evidence={ECO:0000256|ARBA:ARBA00001175,
CC ECO:0000256|RuleBase:RU361204};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU361204};
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005003}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|RuleBase:RU361204}.
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DR EMBL; DS027696; EAW18384.1; -; Genomic_DNA.
DR RefSeq; XP_001260281.1; XM_001260280.1.
DR AlphaFoldDB; A1DG77; -.
DR STRING; 331117.A1DG77; -.
DR EnsemblFungi; EAW18384; EAW18384; NFIA_083350.
DR GeneID; 4586838; -.
DR KEGG; nfi:NFIA_083350; -.
DR VEuPathDB; FungiDB:NFIA_083350; -.
DR eggNOG; KOG1252; Eukaryota.
DR HOGENOM; CLU_021018_0_0_1; -.
DR OMA; TANSPCE; -.
DR OrthoDB; 5487987at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:UniProtKB-UniRule.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:UniProtKB-UniRule.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0019346; P:transsulfuration; IEA:EnsemblFungi.
DR GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IEA:EnsemblFungi.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01137; cysta_beta; 1.
DR PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR PANTHER; PTHR10314:SF194; CYSTATHIONINE BETA-SYNTHASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF00291; PALP; 1.
DR SMART; SM00116; CBS; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51371; CBS; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU361204};
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|RuleBase:RU361204};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361204};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU361204};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702}.
FT DOMAIN 369..426
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 534 AA; 57822 MW; 78F96FEE36354BE3 CRC64;
MSSKTSPAVP PVALDAITQH IGNTPLVRLN RVPQSLGIEA TVYAKLEYFN AGGSVKDRIA
LRMIEEAERS GRIKPGDTLI EPTSGNTGIG LALVAAVKGY KTIITLPEKM SAEKVSVLRA
LNATIIRTPN EAAYDSPESH IGVAKRLEKE IPNAHILDQY GNVNNPLAHE LGTAEEIWTQ
TDGKISAIVA GAGTGGTITG LARGLKKHNP KVKVIAADPH GSILAVPADL NKEHENEPYK
VEGIGYDFIP QVLDQNVVDK WYKTGDRESF QYARRLIAEE GLLVGGSSGS AISALVQAAT
EHTFSKDDVV VVILPDSIRS YLTKFADDDW LAANDLLPSL SSETTLVSQS VQPQAPKDKF
AGAKVKSLRL KPITTVRSNI PCENAIEIMR DRGFDQLPVL APSGKKLVGL VTLGNVLSRL
THGRATKKSL VADVMFDFGK ISEVVTDPRD LGLAESKLSG DQQNGADVLR PQAKNRKFME
ITMDTPLSVL NRFFEWNSAA IVTERDEHGT MRPLAVATKV DLLTWMLHHN EDSS
//
