ID   MAT2B_XENLA             Reviewed;         334 AA.
AC   Q4QQZ4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE   AltName: Full=Methionine adenosyltransferase II beta;
DE            Short=MAT II beta;
GN   Name=mat2b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of S-adenosylmethionine synthetase 2, an
CC       enzyme that catalyzes the formation of S-adenosylmethionine from
CC       methionine and ATP. Regulates MAT2A catalytic activity by changing its
CC       kinetic properties, increasing its affinity for L-methionine. Can bind
CC       NADP (in vitro). {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC       S-adenosyl-L-methionine from L-methionine: step 1/1.
CC       {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- SUBUNIT: Heterotrimer; composed of a catalytic mat2a homodimer that
CC       binds one regulatory mat2b chain. Heterohexamer; composed of a central,
CC       catalytic mat2a homotetramer flanked on either side by a regulatory
CC       mat2b chain. NADP binding increases the affinity for mat2a.
CC       {ECO:0000250|UniProtKB:Q9NZL9}.
CC   -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC       MAT2B subfamily. {ECO:0000305}.
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DR   EMBL; BC097788; AAH97788.1; -; mRNA.
DR   RefSeq; NP_001089523.1; NM_001096054.1.
DR   AlphaFoldDB; Q4QQZ4; -.
DR   SMR; Q4QQZ4; -.
DR   DNASU; 734577; -.
DR   GeneID; 734577; -.
DR   KEGG; xla:734577; -.
DR   CTD; 734577; -.
DR   Xenbase; XB-GENE-972027; mat2b.L.
DR   OrthoDB; 1007850at2759; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 734577; Expressed in testis and 19 other tissues.
DR   GO; GO:0048269; C:methionine adenosyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0048270; F:methionine adenosyltransferase regulator activity; ISS:UniProtKB.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029903; RmlD-like-bd.
DR   PANTHER; PTHR10491; PTHR10491; 1.
DR   Pfam; PF04321; RmlD_sub_bind; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   NADP; One-carbon metabolism; Reference proteome.
FT   CHAIN           1..334
FT                   /note="Methionine adenosyltransferase 2 subunit beta"
FT                   /id="PRO_0000287525"
FT   REGION          319..334
FT                   /note="Required for interaction with MAT2A"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         37..40
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         60..62
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         71..72
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         93
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         97
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT   BINDING         159
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZL9"
SQ   SEQUENCE   334 AA;  37641 MW;  4FADFEB816B712AB CRC64;
     MEGRYKDYRI RFSPGWVEVV QDDVTVPSRR ALITGATGLL GRAVYKEFKE NSWHVLGCGY
     SRARPRFECL NLLDEAAVKA LIQDFKPHVI IHCAAERRPD IVESQPELAS LLNVVASENL
     AKVAAGVGAF LIYVSSDYVF DGTSPPYRED SIPHPLNLYG KTKLDGERAV LQNNEGAAVL
     RVPVMYGDVE KLSESAVTIL FDKVQFSNKS ANLDHCQQRF PTHVKDVATV CLQLTERKIQ
     DPSIKGIYHW SGNEQMTKYE IACAMADAFN LPSSHLRPIT DEPVGATPRP WNPQLDCSKL
     EKMGIGQRTP FRVGIRETLW PFLVDKRWRQ TVFH