MFNC_METJA
ID MFNC_METJA Reviewed; 370 AA.
AC Q58097;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate transaminase {ECO:0000305};
DE EC=2.6.1.108 {ECO:0000269|PubMed:24977328};
DE AltName: Full=4-HFC-P:alanine aminotransferase {ECO:0000303|PubMed:24977328};
GN Name=mfnC {ECO:0000303|PubMed:24977328}; OrderedLocusNames=MJ0684;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24977328; DOI=10.1021/bi500615p;
RA Miller D., Wang Y., Xu H., Harich K., White R.H.;
RT "Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of
RT methanofuran.";
RL Biochemistry 53:4635-4647(2014).
RN [3]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=12595727; DOI=10.1107/s0907444903000076;
RA Yang J.K., Chang C., Cho S.J., Lee J.Y., Yu Y.G., Eom S.H., Suh S.W.;
RT "Crystallization and preliminary X-ray analysis of the Mj0684 gene product,
RT a putative aspartate aminotransferase, from Methanococcus jannaschii.";
RL Acta Crystallogr. D 59:563-565(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL-PHOSPHATE,
RP COFACTOR, AND SUBUNIT.
RX DOI=10.5012/bkcs.2008.29.1.173;
RA Yang J.K.;
RT "Crystal structure of MJ0684 from Methanococcus jannaschii, a novel
RT archaeal homolog of kynurenine aminotransferase.";
RL Bull. Korean Chem. Soc. 29:173-176(2008).
CC -!- FUNCTION: Catalyzes the transamination reaction between 4-
CC (hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) and alanine
CC to produce pyruvate and 5-(aminomethyl)-3-furanmethanol phosphate (F1-
CC P), the precursor for the furan moiety in methanofuran.
CC {ECO:0000269|PubMed:24977328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-(hydroxymethyl)-2-furancarboxaldehyde phosphate + L-alanine
CC = [5-(aminomethyl)-3-furyl]methyl phosphate + pyruvate;
CC Xref=Rhea:RHEA:43564, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:83407, ChEBI:CHEBI:83431; EC=2.6.1.108;
CC Evidence={ECO:0000269|PubMed:24977328};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|Ref.4};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000269|PubMed:24977328}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12595727, ECO:0000269|Ref.4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L77117; AAB98679.1; -; Genomic_DNA.
DR RefSeq; WP_010870189.1; NC_000909.1.
DR PDB; 2Z61; X-ray; 2.20 A; A=1-370.
DR PDBsum; 2Z61; -.
DR AlphaFoldDB; Q58097; -.
DR SMR; Q58097; -.
DR STRING; 243232.MJ_0684; -.
DR EnsemblBacteria; AAB98679; AAB98679; MJ_0684.
DR GeneID; 1451550; -.
DR KEGG; mja:MJ_0684; -.
DR eggNOG; arCOG01130; Archaea.
DR HOGENOM; CLU_017584_4_3_2; -.
DR InParanoid; Q58097; -.
DR OMA; WIVADEV; -.
DR OrthoDB; 32104at2157; -.
DR PhylomeDB; Q58097; -.
DR BioCyc; MetaCyc:MON-18938; -.
DR BRENDA; 2.6.1.108; 3260.
DR UniPathway; UPA00080; -.
DR EvolutionaryTrace; Q58097; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..370
FT /note="(5-formylfuran-3-yl)methyl phosphate transaminase"
FT /id="PRO_0000123859"
FT MOD_RES 222
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|Ref.4"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 125..132
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:2Z61"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:2Z61"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 238..251
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 269..295
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2Z61"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:2Z61"
FT HELIX 354..368
FT /evidence="ECO:0007829|PDB:2Z61"
SQ SEQUENCE 370 AA; 42348 MW; 51C2EE6D50079940 CRC64;
MLSKRLLNFE SFEVMDILAL AQKLESEGKK VIHLEIGEPD FNTPKPIVDE GIKSLKEGKT
HYTDSRGILE LREKISELYK DKYKADIIPD NIIITGGSSL GLFFALSSII DDGDEVLIQN
PCYPCYKNFI RFLGAKPVFC DFTVESLEEA LSDKTKAIII NSPSNPLGEV IDREIYEFAY
ENIPYIISDE IYNGLVYEGK CYSAIEFDEN LEKTILINGF SKLYAMTGWR IGYVISNDEI
IEAILKLQQN LFISAPTISQ YAALKAFEKE TEREINSMIK EFDRRRRLVL KYVKDFGWEV
NNPIGAYYVF PNIGEDGREF AYKLLKEKFV ALTPGIGFGS KGKNYIRISY ANSYENIKEG
LERIKEFLNK
