ID A0A1Z5T615_HORWE Unreviewed; 950 AA.
AC A0A1Z5T615;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000256|ARBA:ARBA00026192, ECO:0000256|RuleBase:RU361204};
DE EC=4.2.1.22 {ECO:0000256|RuleBase:RU361204};
GN ORFNames=BTJ68_10048 {ECO:0000313|EMBL:OTA31291.1};
OS Hortaea werneckii EXF-2000.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA31291.1, ECO:0000313|Proteomes:UP000194280};
RN [1] {ECO:0000313|EMBL:OTA31291.1, ECO:0000313|Proteomes:UP000194280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA31291.1,
RC ECO:0000313|Proteomes:UP000194280};
RA Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA Nislow C.E.;
RT "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT insights from long-read sequencing.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol 1-phosphate + NAD(+) = beta-D-fructose 6-phosphate
CC + H(+) + NADH; Xref=Rhea:RHEA:19661, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57634, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:61381; EC=1.1.1.17;
CC Evidence={ECO:0000256|ARBA:ARBA00000292};
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|RuleBase:RU361204};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000256|RuleBase:RU361204}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00006541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTA31291.1}.
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DR EMBL; MUNK01000117; OTA31291.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5T615; -.
DR STRING; 1157616.A0A1Z5T615; -.
DR VEuPathDB; FungiDB:BTJ68_10048; -.
DR InParanoid; A0A1Z5T615; -.
DR OrthoDB; 1700931at2759; -.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000194280; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008926; F:mannitol-1-phosphate 5-dehydrogenase activity; IEA:UniProtKB-EC.
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:0019594; P:mannitol metabolic process; IEA:InterPro.
DR CDD; cd01561; CBS_like; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00196; Mannitol_dehydrog; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR023028; Mannitol_1_phos_5_DH.
DR InterPro; IPR000669; Mannitol_DH.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PTHR30524:SF0; ALTRONATE OXIDOREDUCTASE-RELATED; 1.
DR PANTHER; PTHR30524; MANNITOL-1-PHOSPHATE 5-DEHYDROGENASE; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR Pfam; PF00291; PALP; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SMART; SM00116; CBS; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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}; Lyase {ECO:0000256|RuleBase:RU361204};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Pyridoxal phosphate {ECO:0000256|RuleBase:RU361204};
KW Reference proteome {ECO:0000313|Proteomes:UP000194280}.
FT DOMAIN 389..450
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 329..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 104288 MW; 803BB62B69304EB2 CRC64;
MDSILQNIGN TPLVRLNRIP QSAGIKCNIY AKCEFFNAGG SVKDRIALRM VEAAEKEGRL
TPGHSVLIEP TSGNTGIGLA LVGAVKGYRT IITLPEKMSS EKVSVLKALG AEIIRTPTSA
AWDSPESHIG VARRLEKEIP GGVILDQYSN PNNPMAHEMG TAKEIVDQME QVEGRLAAVI
AGAGTGGTVT GLSRGVRKAH GDKVKIVAAD PHGSILALPA SLNDEHNGAS YKVEGIGYDF
IPDVLGQQEV DKWYKTDDRE SFYWARRLIR EEGLLVGGSS GSAMTACMKA IHDMKLGENE
SIVVILPDSI RSYLSKFVDD DWLAANDLLP PSPPLTAPSS PKMESNDKSG QEMKVVVPNG
NTHQPPTSPT HARKSSRDEY ANATVRDLRL KPIQTITSSQ TVDEAVELMR DKGYDQIPVT
SSSNRRLVGL VTLGNCLSYL SSKKIHITDP VEKVMFNFSK MDEVRPLEKH QGLTEGDETK
REFAEITMET SLRALERFLT WNAAAIVTER TDEKALKPLA VVTKVDLLVC CAGDLFGFIP
KASLQILFCA YHVIKFISNS TMAGKKGVHF GGGNIGRGFV AEFLHNSGYE VVFIDVMDAI
IEKLQNAKSY EVKEIGPSGE KTFTIDNYRA LNSKYDMEKV IHEIATADTV TCAVGPNILK
FIAEPIAKGI ESRESSTPVA VIACENAIGA TDNLKGFIME KLSDDTKSKL NSKARFANSA
VDRIVPIQDE DAGLNVKIEQ FFEWCVESPP FEGNPPDIQG VHYVQDLQPY IERKLFTVNT
GHATAAYYGH HRGIKYIHEV LENKELQEIV QNTLKETAHL ICSKHDHISK EEQQDYVQKI
VTRISNPVLK DGVDRVGRAP LRKLSRKERF IGPAAHLAEM GEKYDYLLGG IEMALRFQNV
EGDDESVELA KILKDNDANA ATKKLTGLEE THPIFAKVSE VVAKVQKETA
//
