MAP1B_ARATH
ID MAP1B_ARATH Reviewed; 369 AA.
AC Q9FV52; Q9FX70;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Methionine aminopeptidase 1B, chloroplastic {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MAP 1B {ECO:0000255|HAMAP-Rule:MF_03174};
DE Short=MetAP 1B {ECO:0000255|HAMAP-Rule:MF_03174};
DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_03174};
DE AltName: Full=Peptidase M 1B {ECO:0000255|HAMAP-Rule:MF_03174};
DE Flags: Precursor;
GN Name=MAP1B; OrderedLocusNames=At1g13270; ORFNames=T6J4.3;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11060042; DOI=10.1093/emboj/19.21.5916;
RA Giglione C., Serero A., Pierre M., Boisson B., Meinnel T.;
RT "Identification of eukaryotic peptide deformylases reveals universality of
RT N-terminal protein processing mechanisms.";
RL EMBO J. 19:5916-5929(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. The
CC N-terminal methionine is often cleaved when the second residue in the
CC primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser,
CC Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03174}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal amino acids, preferentially methionine,
CC from peptides and arylamides.; EC=3.4.11.18;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03174};
CC Note=Binds 2 divalent metal cations per subunit. Has a high-affinity
CC and a low affinity metal-binding site. The true nature of the
CC physiological cofactor is under debate. The enzyme is active with
CC cobalt, zinc, manganese or divalent iron ions. Most likely, methionine
CC aminopeptidases function as mononuclear Fe(2+)-metalloproteases under
CC physiological conditions, and the catalytically relevant metal-binding
CC site has been assigned to the histidine-containing high-affinity site.
CC {ECO:0000255|HAMAP-Rule:MF_03174};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_03174, ECO:0000269|PubMed:11060042}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FV52-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Preferentially expressed in green
CC tissues. {ECO:0000269|PubMed:11060042}.
CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine
CC aminopeptidase type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_03174}.
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DR EMBL; AF250961; AAG33975.1; -; mRNA.
DR EMBL; AC011810; AAG09564.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28993.1; -; Genomic_DNA.
DR EMBL; BT000449; AAN17426.1; -; mRNA.
DR EMBL; BT001213; AAN65100.1; -; mRNA.
DR PIR; C86267; C86267.
DR RefSeq; NP_172785.1; NM_101198.4. [Q9FV52-1]
DR AlphaFoldDB; Q9FV52; -.
DR SMR; Q9FV52; -.
DR BioGRID; 23127; 2.
DR IntAct; Q9FV52; 1.
DR STRING; 3702.AT1G13270.1; -.
DR MEROPS; M24.A05; -.
DR PaxDb; Q9FV52; -.
DR PRIDE; Q9FV52; -.
DR ProteomicsDB; 238281; -. [Q9FV52-1]
DR EnsemblPlants; AT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
DR GeneID; 837887; -.
DR Gramene; AT1G13270.1; AT1G13270.1; AT1G13270. [Q9FV52-1]
DR KEGG; ath:AT1G13270; -.
DR Araport; AT1G13270; -.
DR TAIR; locus:2205329; AT1G13270.
DR eggNOG; KOG2738; Eukaryota.
DR HOGENOM; CLU_015857_1_5_1; -.
DR InParanoid; Q9FV52; -.
DR OMA; CKHGASY; -.
DR OrthoDB; 1002357at2759; -.
DR PhylomeDB; Q9FV52; -.
DR PRO; PR:Q9FV52; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FV52; baseline and differential.
DR Genevisible; Q9FV52; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; TAS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0031365; P:N-terminal protein amino acid modification; TAS:TAIR.
DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01086; MetAP1; 1.
DR Gene3D; 3.90.230.10; -; 1.
DR HAMAP; MF_01974; MetAP_1; 1.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001714; Pept_M24_MAP.
DR InterPro; IPR002467; Pept_M24A_MAP1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; SSF55920; 1.
DR TIGRFAMs; TIGR00500; met_pdase_I; 1.
DR PROSITE; PS00680; MAP_1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Aminopeptidase; Chloroplast; Hydrolase;
KW Metal-binding; Plastid; Protease; Reference proteome; Transit peptide.
FT TRANSIT 1..61
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 62..369
FT /note="Methionine aminopeptidase 1B, chloroplastic"
FT /id="PRO_0000045805"
FT BINDING 199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 227
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 227
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 290
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 297
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 322
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 353
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT BINDING 353
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03174"
FT CONFLICT 34
FT /note="L -> I (in Ref. 1; AAG33975)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="R -> Q (in Ref. 1; AAG33975)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="R -> K (in Ref. 1; AAG33975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40424 MW; 0D28974852F33747 CRC64;
MASSVFLSSF SSSSSLQLCS SFHGEYLAPS RCFLGAPVTS SSLSLSGKKN SYSPRQFHVS
AKKVSGLEEA IRIRKMRELE TKSKVRRNPP LRRGRVSPRL LVPDHIPRPP YVESGVLPDI
SSEFQIPGPE GIAKMRAACE LAARVLNYAG TLVKPSVTTN EIDKAVHDMI IEAGAYPSPL
GYGGFPKSVC TSVNECMCHG IPDSRQLQSG DIINIDVTVY LDGYHGDTSR TFFCGEVDEG
FKRLVKVTEE CLERGIAVCK DGASFKKIGK RISEHAEKFG YNVVERFVGH GVGPVFHSEP
LIYHYRNDEP GLMVEGQTFT IEPILTIGTT ECVTWPDNWT TLTADGGVAA QFEHTILITR
TGSEILTKC
