ID G2HG86_PANTR Unreviewed; 323 AA.
AC G2HG86; A0A2J8NKN6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Methionine adenosyltransferase 2 subunit beta {ECO:0000256|ARBA:ARBA00021596, ECO:0000256|RuleBase:RU364081};
DE AltName: Full=Methionine adenosyltransferase II beta {ECO:0000256|ARBA:ARBA00029977, ECO:0000256|RuleBase:RU364081};
GN Name=MAT2B {ECO:0000313|EMBL:JAA04661.1,
GN ECO:0000313|Ensembl:ENSPTRP00000090127.1, ECO:0000313|VGNC:VGNC:7085};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|EMBL:BAK62744.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000090127.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|EMBL:BAK62744.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Testis {ECO:0000313|EMBL:BAK62744.1};
RX PubMed=21484476; DOI=10.1007/s10142-011-0220-9;
RA Kim R.N., Kim D.W., Choi S.H., Chae S.H., Nam S.H., Kim D.W., Kim A.,
RA Kang A., Park K.H., Lee Y.S., Hirai M., Suzuki Y., Sugano S., Hashimoto K.,
RA Kim D.S., Park H.S.;
RT "Major chimpanzee-specific structural changes in sperm development-
RT associated genes.";
RL Funct. Integr. Genomics 11:507-517(2011).
RN [3] {ECO:0000313|EMBL:JAA04661.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Adipose stromal {ECO:0000313|EMBL:JAA04661.1}, Skeletal muscle
RC {ECO:0000313|EMBL:JAA36836.1}, Skin {ECO:0000313|EMBL:JAA24303.1}, and
RC Smooth vascular {ECO:0000313|EMBL:JAA15623.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSPTRP00000090127.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|RuleBase:RU364081}.
CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis;
CC S-adenosyl-L-methionine from L-methionine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005224, ECO:0000256|RuleBase:RU364081}.
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:0000256|RuleBase:RU364081}.
CC -!- SIMILARITY: Belongs to the dTDP-4-dehydrorhamnose reductase family.
CC MAT2B subfamily. {ECO:0000256|ARBA:ARBA00008656,
CC ECO:0000256|RuleBase:RU364081}.
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DR EMBL; AACZ04059019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK305750; BAK62744.1; -; mRNA.
DR EMBL; GABC01006677; JAA04661.1; -; mRNA.
DR EMBL; GABF01006522; JAA15623.1; -; mRNA.
DR EMBL; GABD01008797; JAA24303.1; -; mRNA.
DR EMBL; GABE01007903; JAA36836.1; -; mRNA.
DR RefSeq; NP_001233495.1; NM_001246566.1.
DR Ensembl; ENSPTRT00000101839.1; ENSPTRP00000090127.1; ENSPTRG00000017504.5.
DR GeneID; 462245; -.
DR KEGG; ptr:462245; -.
DR CTD; 27430; -.
DR VGNC; VGNC:7085; MAT2B.
DR GeneTree; ENSGT00390000006721; -.
DR OMA; IRTAWVY; -.
DR OrthoDB; 3080056at2759; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017504; Expressed in fibroblast and 21 other cell types or tissues.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05254; dTDP_HR_like_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR005913; dTDP_dehydrorham_reduct.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR029903; RmlD-like-bd.
DR PANTHER; PTHR10491; DTDP-4-DEHYDRORHAMNOSE REDUCTASE; 1.
DR PANTHER; PTHR10491:SF4; METHIONINE ADENOSYLTRANSFERASE 2 SUBUNIT BETA; 1.
DR Pfam; PF04321; RmlD_sub_bind; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU364081};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Transferase {ECO:0000313|EMBL:BAK62744.1}.
FT DOMAIN 19..311
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 323 AA; 36401 MW; 4B2197246063E711 CRC64;
MPEMPEDMEQ EEVNIPNRRV LVTGATGLLG RAVHKEFQQN NWHAVGCGFR RARPKFEQVN
LLDSNAVHHI IHDFQPHVIV HCAAERRPDV VENQPDAASQ LNVDASGNLA KEAAAVGAFL
IYISSDYVFD GTNPPYREED IPAPLNLYGK TKLDGEKAVL ENNLGAAVLR IPILYGEVEK
LEESAVTVMF DKVQFSNKSA NMDHWQQRFP THVKDVATVC RQLAEKRMLD PSIKGTFHWS
GNEQMTKYEM ACAIADAFNL PSSHLRPITD SPVLGAQRPR NAQLDCSKLE TLGIGQRTPF
RIGIKESLWP FLIDKRWRQT VFH
//
