ID G1LF26_AILME Unreviewed; 334 AA.
AC G1LF26;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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|Ensembl:ENSAMEP00000005513.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000005513.1, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000005513.1, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000005513.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_002926826.1; XM_002926780.3.
DR AlphaFoldDB; G1LF26; -.
DR STRING; 9646.ENSAMEP00000005513; -.
DR Ensembl; ENSAMET00000005739.2; ENSAMEP00000005513.1; ENSAMEG00000005210.2.
DR GeneID; 100481953; -.
DR CTD; 27430; -.
DR eggNOG; KOG1430; Eukaryota.
DR GeneTree; ENSGT00390000006721; -.
DR HOGENOM; CLU_045518_0_0_1; -.
DR InParanoid; G1LF26; -.
DR OMA; IRTAWVY; -.
DR OrthoDB; 3080056at2759; -.
DR TreeFam; TF332849; -.
DR UniPathway; UPA00315; UER00080.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0048269; C:methionine adenosyltransferase complex; IEA:Ensembl.
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; IEA:Ensembl.
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 3: Inferred from homology;
KW One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW ECO:0000256|RuleBase:RU364081};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912}.
FT DOMAIN 30..322
FT /note="RmlD-like substrate binding"
FT /evidence="ECO:0000259|Pfam:PF04321"
SQ SEQUENCE 334 AA; 37673 MW; 149FC8E0B9DE5A57 CRC64;
MVGRENELSI HFVPGSCRLV EEEVNVPNRR VLITGATGLL GRAVYKEFKQ NNWHAFGCGF
RRARPKFEQV NLLDSEAVHH IIHDFQPHVI VHCAAERRPD VVENQPDAAS QLNVDASGNL
AKEAASIGAF LIYISSDYVF DGTNPPYREE DVPSPLNLYG KTKLEGEKAV LENNLGAAVL
RIPVLYGEVE KLEESAVTVM FDKVQFSNKS ANMDHWQQRF PTHVKDVATV CRQLAEKRML
DPSIKGTFHW SGNEQMTKYE MACAIADAFN LPSSHLRPIT DSPVLGAQRP RNAQLDCTKL
ETLGIGQRTP FRIGIKESLW PFLIDKRWRQ TVFH
//