MAT2B_PONAB
ID MAT2B_PONAB Reviewed; 334 AA.
AC Q5R4E0; Q5R8E6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Methionine adenosyltransferase 2 subunit beta;
DE AltName: Full=Methionine adenosyltransferase II beta;
DE Short=MAT II beta;
GN Name=MAT2B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5R4E0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5R4E0-2; Sequence=VSP_025544;
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC MAT2B subfamily. {ECO:0000305}.
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DR EMBL; CR861310; CAH93376.1; -; mRNA.
DR EMBL; CR859806; CAH91964.1; -; mRNA.
DR RefSeq; NP_001126137.1; NM_001132665.1.
DR RefSeq; XP_009239534.1; XM_009241259.1. [Q5R4E0-1]
DR AlphaFoldDB; Q5R4E0; -.
DR SMR; Q5R4E0; -.
DR STRING; 9601.ENSPPYP00000017930; -.
DR Ensembl; ENSPPYT00000039719; ENSPPYP00000037996; ENSPPYG00000016020. [Q5R4E0-2]
DR GeneID; 100173095; -.
DR KEGG; pon:100173095; -.
DR CTD; 27430; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00390000006721; -.
DR HOGENOM; CLU_045518_0_0_1; -.
DR InParanoid; Q5R4E0; -.
DR OMA; AGETTWH; -.
DR TreeFam; TF332849; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
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 Alternative splicing; NADP; One-carbon metabolism; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..334
FT /note="Methionine adenosyltransferase 2 subunit beta"
FT /id="PRO_0000287522"
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"
FT BINDING 185
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZL9"
FT VAR_SEQ 1..21
FT /note="MVGREKELSIHFVPGSCRLVE -> MPEMPEDMEQ (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_025544"
FT CONFLICT 25
FT /note="N -> S (in Ref. 1; CAH91964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37552 MW; 6AAA5381BAF3F65F CRC64;
MVGREKELSI HFVPGSCRLV EEEVNIPNRR VLVTGATGLL GRAVHKEFQQ NNWHAVGCGF
RRARPKFEQV NLLDSNAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL
AKEAAAVGAF LIYISSDYVF DGTNPPYREE DIPAPLNLYG KTKLDGEKAV LENNLGAAVL
RIPILYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML
DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCSKL
ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH
