CBS_APIME
ID CBS_APIME Reviewed; 504 AA.
AC Q2V0C9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Cystathionine beta-synthase {ECO:0000303|PubMed:29275181};
DE EC=4.2.1.22 {ECO:0000269|PubMed:29275181};
GN Name=CBS {ECO:0000303|PubMed:29275181};
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; Apidae;
OC Apis.
OX NCBI_TaxID=7460 {ECO:0000312|EMBL:BAE66603.1};
RN [1] {ECO:0000312|EMBL:BAE66603.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAE66603.1};
RA Watanabe T., Shiga T., Yamamoto T., Suzuki N., Ito E.;
RT "Molecular cloning of NOS, sGC, CBS and HO genes in Honey bee brain.";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5OHX}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND HEME, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND
RP SUBUNIT.
RX PubMed=29275181; DOI=10.1016/j.jsb.2017.12.008;
RA Gimenez-Mascarell P., Majtan T., Oyenarte I., Ereno-Orbea J., Majtan J.,
RA Klaudiny J., Kraus J.P., Martinez-Cruz L.A.;
RT "Crystal structure of cystathionine beta-synthase from honeybee Apis
RT mellifera.";
RL J. Struct. Biol. 202:82-93(2018).
CC -!- FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration
CC pathway, where the hydroxyl group of L-serine is displaced by L-
CC homocysteine in a beta-replacement reaction to form L-cystathionine,
CC the precursor of L-cysteine. {ECO:0000269|PubMed:29275181}.
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:0000269|PubMed:29275181};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P35520};
CC -!- ACTIVITY REGULATION: Has no response to S-adenosyl-methionine/AdoMet,
CC unlike mammalian orthologs (PubMed:29275181). Binds non-covalently to a
CC heme group that may control the redox sensitivity of the enzyme (By
CC similarity). {ECO:0000250|UniProtKB:P35520,
CC ECO:0000269|PubMed:29275181}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC from L-homocysteine and L-serine: step 1/2.
CC {ECO:0000269|PubMed:29275181}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:29275181}.
CC -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC synthase family. {ECO:0000305}.
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DR EMBL; AB244761; BAE66603.1; -; mRNA.
DR RefSeq; NP_001035353.1; NM_001040263.1.
DR PDB; 5OHX; X-ray; 3.20 A; A/B=1-504.
DR PDBsum; 5OHX; -.
DR AlphaFoldDB; Q2V0C9; -.
DR SMR; Q2V0C9; -.
DR EnsemblMetazoa; NM_001040263; NP_001035353; GeneID_551341.
DR GeneID; 551341; -.
DR KEGG; ame:551341; -.
DR CTD; 875; -.
DR OrthoDB; 1016546at2759; -.
DR PhylomeDB; Q2V0C9; -.
DR BRENDA; 4.2.1.22; 387.
DR UniPathway; UPA00136; UER00201.
DR Proteomes; UP000005203; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004122; F:cystathionine beta-synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0006535; P:cysteine biosynthetic process from serine; IDA:UniProtKB.
DR GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IDA:UniProtKB.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR005857; Cysta_beta_synth.
DR InterPro; IPR001216; P-phosphate_BS.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR01137; cysta_beta; 1.
DR PROSITE; PS00901; CYS_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; CBS domain; Cysteine biosynthesis;
KW Heme; Iron; Isopeptide bond; Lyase; Metal-binding; Pyridoxal phosphate;
KW Reference proteome.
FT CHAIN 1..504
FT /note="Cystathionine beta-synthase"
FT /id="PRO_0000451741"
FT DOMAIN 375..434
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 442..498
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 12
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:29275181"
FT BINDING 23
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000269|PubMed:29275181"
FT BINDING 108
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:29275181"
FT BINDING 215..219
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:29275181"
FT BINDING 307
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:29275181"
FT MOD_RES 78
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:29275181"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 78..91
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5OHX"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:5OHX"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:5OHX"
FT TURN 336..343
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 346..351
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 362..366
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 438..441
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 455..461
FT /evidence="ECO:0007829|PDB:5OHX"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:5OHX"
FT TURN 473..477
FT /evidence="ECO:0007829|PDB:5OHX"
FT STRAND 478..483
FT /evidence="ECO:0007829|PDB:5OHX"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:5OHX"
SQ SEQUENCE 504 AA; 56221 MW; CE4D25D6D410876E CRC64;
MEFKQPNRPS YCTWELNATN SPHTCRTKNG DYTKIMPDIL TAIGQTPLIK LNNIPKSYGI
KCEIYAKCEF LNPGGSVKDR IAYRMIQDAE DKGLLKPGCT IIEPTSGNTG IGLAMAAAVR
GYKCIIVMPE KMSDEKISTL YALGAKIIRT PTEASWHSPE AHISVAQKLQ KEIPNSIILD
QYTNPGNPLA HYDQTAIEIW KQCEGKIDYL VAGAGTGGTI SGIGRKLKEL SPNIKIIAVD
PKGSILDPSS DSQNEVGFYE VEGIGYDFIP TVLDRNVIDK WIKTEDNESL NAARMLIRQE
GLLCGGSSGA ALIAALKIAK DIPEEKRMVI ILPDGIRNYL TKFVSEYWME TRGFLQPVCQ
NEMNKWWWNM KISNLSFDKQ SLLKENTVTC QEAMHMLKNA DSQLLVISDD NIHIKGVISL
NKLTSYVISG IVKCTDFVDK AMVKQYVKVK HSATLGYISR VLEKEPYVII LDDEHDDAFI
GIVNQFHILQ FITKNGTSNN YLIN
