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Entry: A0A091PLK4_HALAL
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ID   A0A091PLK4_HALAL        Unreviewed;       313 AA.
AC   A0A091PLK4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 28.
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};
DE   Flags: Fragment;
GN   Name=Mat2b {ECO:0000313|EMBL:NWZ56524.1};
GN   ORFNames=HALALB_R04481 {ECO:0000313|EMBL:NWZ56524.1}, N329_07068
GN   {ECO:0000313|EMBL:KFQ08221.1};
OS   Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Haliaeetus.
OX   NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ08221.1, ECO:0000313|Proteomes:UP000054379};
RN   [1] {ECO:0000313|EMBL:KFQ08221.1, ECO:0000313|Proteomes:UP000054379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ08221.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:NWZ56524.1, ECO:0000313|Proteomes:UP000585422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OUT-0040 {ECO:0000313|EMBL:NWZ56524.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:NWZ56524.1};
RA   Zhang G.;
RT   "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL   Submitted (SEP-2019) 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.
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; KK661035; KFQ08221.1; -; Genomic_DNA.
DR   EMBL; VZSQ01000178; NWZ56524.1; -; Genomic_DNA.
DR   RefSeq; XP_009922384.1; XM_009924082.1.
DR   GeneID; 104321417; -.
DR   KEGG; hald:104321417; -.
DR   CTD; 27430; -.
DR   OrthoDB; 3080056at2759; -.
DR   UniPathway; UPA00315; UER00080.
DR   Proteomes; UP000054379; Unassembled WGS sequence.
DR   Proteomes; UP000585422; Unassembled WGS sequence.
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   3: Inferred from homology;
KW   One-carbon metabolism {ECO:0000256|ARBA:ARBA00022563,
KW   ECO:0000256|RuleBase:RU364081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW   Transferase {ECO:0000313|EMBL:KFQ08221.1}.
FT   DOMAIN          9..301
FT                   /note="RmlD-like substrate binding"
FT                   /evidence="ECO:0000259|Pfam:PF04321"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ08221.1"
FT   NON_TER         313
FT                   /evidence="ECO:0000313|EMBL:KFQ08221.1"
SQ   SEQUENCE   313 AA;  35047 MW;  7585345227C0DCF1 CRC64;
     EDVHIPSRRV LITGATGLLG RAVFKEFNEN NWNAVGCGYR RAQPRFEQIN LLDSIAVHDI
     IHDFQPHVIV HCAAERRPDV VESQPDAASQ LNVAASGNLA KEAAGVGAFL IYISTDYVFD
     GTSPPYKETD VPNPLNLYGK TKLEGEKAVL ENNEDAAVLR IPVLYGDVER LEESAVTVMF
     DKVQFSNKSA NMDHWQQRFP TNVKDVATVC RQLAEKRMLD PSVKGTFHWS GNEQMTKYEM
     ACAIADAFNL PSSHLRPITD CPVVGALRPR NAQLDCSKLE MLGIGQRTPF RAGIKESLWP
     FLVDKRWRQT VFH
//
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