ID A0A091KFB3_9GRUI Unreviewed; 223 AA.
AC A0A091KFB3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Methylthioribulose-1-phosphate dehydratase {ECO:0000313|EMBL:KFP38802.1};
DE Flags: Fragment;
GN ORFNames=N324_04712 {ECO:0000313|EMBL:KFP38802.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP38802.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP38802.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP38802.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the aldolase class II family. Adducin subfamily.
CC {ECO:0000256|ARBA:ARBA00006274}.
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DR EMBL; KK741100; KFP38802.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091KFB3; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:InterPro.
DR Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR HAMAP; MF_03116; Salvage_MtnB_euk; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR InterPro; IPR017714; MethylthioRu-1-P_deHdtase_MtnB.
DR InterPro; IPR027514; Salvage_MtnB_euk.
DR NCBIfam; TIGR03328; salvage_mtnB; 1.
DR PANTHER; PTHR10640; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR PANTHER; PTHR10640:SF7; METHYLTHIORIBULOSE-1-PHOSPHATE DEHYDRATASE; 1.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000053330};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..203
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP38802.1"
FT NON_TER 223
FT /evidence="ECO:0000313|EMBL:KFP38802.1"
SQ SEQUENCE 223 AA; 25090 MW; 28A00944E02D5E85 CRC64;
EKLHPRNLIP ELCRLFYGLG WVTGTGGGIS LKHGNEIYIA PSGVQKERIQ PEDMFVCDMN
EKDISGPPPH KKLKKSQCTP LFMNAYTMRG AGAVIHTHSK AAVMATLLYP GSEFSITHQE
MIKGIQKCTS GGYYRYDDTL VVPIIENTPE EKDLKERMAH AMEKYPDSCA VLVRRHGVYV
WGETWEKAKT MCECYDYLFD IAVQMKQHGL DPSKHPAGEN GIL
//
