ID   F2LXX8_HIPMA            Unreviewed;       412 AA.
AC   F2LXX8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   02-SEP-2026, entry version 79.
DE   RecName: Full=Diaminopimelate decarboxylase {ECO:0000256|ARBA:ARBA00074972, ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAP decarboxylase {ECO:0000256|HAMAP-Rule:MF_02120};
DE            Short=DAPDC {ECO:0000256|HAMAP-Rule:MF_02120};
DE            EC=4.1.1.20 {ECO:0000256|ARBA:ARBA00066427, ECO:0000256|HAMAP-Rule:MF_02120};
GN   Name=lysA {ECO:0000256|HAMAP-Rule:MF_02120};
GN   OrderedLocusNames=Hipma_0266 {ECO:0000313|EMBL:AEA33243.1};
OS   Hippea maritima (strain ATCC 700847 / DSM 10411 / MH2).
OC   Bacteria; Pseudomonadati; Campylobacterota; Desulfurellia; Desulfurellales;
OC   Hippeaceae; Hippea.
OX   NCBI_TaxID=760142 {ECO:0000313|EMBL:AEA33243.1, ECO:0000313|Proteomes:UP000008139};
RN   [1] {ECO:0000313|EMBL:AEA33243.1, ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RX   PubMed=21886857;
RA   Huntemann M., Lu M., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Ivanova N., Ovchinikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Rohde M., Spring S., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Mavromatis K.;
RT   "Complete genome sequence of the thermophilic sulfur-reducer Hippea
RT   maritima type strain (MH(2)).";
RL   Stand. Genomic Sci. 4:303-311(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008139}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700847 / DSM 10411 / MH2
RC   {ECO:0000313|Proteomes:UP000008139};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Mikhailova N., Lu M., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Schroeder M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Hippea maritima DSM 10411.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically catalyzes the decarboxylation of meso-
CC       diaminopimelate (meso-DAP) to L-lysine. {ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=meso-2,6-diaminopimelate + H(+) = L-lysine + CO2;
CC         Xref=Rhea:RHEA:15101, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:32551, ChEBI:CHEBI:57791; EC=4.1.1.20;
CC         Evidence={ECO:0000256|ARBA:ARBA00050464, ECO:0000256|HAMAP-
CC         Rule:MF_02120, ECO:0000256|RuleBase:RU003738};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933, ECO:0000256|HAMAP-
CC         Rule:MF_02120, ECO:0000256|PIRSR:PIRSR600183-50,
CC         ECO:0000256|RuleBase:RU003738};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00060643, ECO:0000256|HAMAP-Rule:MF_02120,
CC       ECO:0000256|RuleBase:RU003738}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_02120}.
CC   -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC       LysA subfamily. {ECO:0000256|ARBA:ARBA00060983, ECO:0000256|HAMAP-
CC       Rule:MF_02120}.
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DR   EMBL; CP002606; AEA33243.1; -; Genomic_DNA.
DR   RefSeq; WP_013681287.1; NC_015318.1.
DR   AlphaFoldDB; F2LXX8; -.
DR   FunCoup; F2LXX8; 345.
DR   STRING; 760142.Hipma_0266; -.
DR   KEGG; hmr:Hipma_0266; -.
DR   eggNOG; COG0019; Bacteria.
DR   HOGENOM; CLU_026444_0_0_7; -.
DR   InParanoid; F2LXX8; -.
DR   OrthoDB; 9802241at2; -.
DR   UniPathway; UPA00034; UER00027.
DR   Proteomes; UP000008139; Chromosome.
DR   GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06828; PLPDE_III_DapDC; 1.
DR   FunFam; 2.40.37.10:FF:000003; Diaminopimelate decarboxylase; 1.
DR   FunFam; 3.20.20.10:FF:000003; Diaminopimelate decarboxylase; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 2.40.37.10; Lyase, Ornithine Decarboxylase, Chain A, domain 1; 1.
DR   HAMAP; MF_02120; LysA; 1.
DR   InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR   InterPro; IPR002986; DAP_deCOOHase_LysA.
DR   InterPro; IPR022643; De-COase2_C.
DR   InterPro; IPR022644; De-COase2_N.
DR   InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   NCBIfam; TIGR01048; lysA; 1.
DR   PANTHER; PTHR43727; DIAMINOPIMELATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43727:SF2; GROUP IV DECARBOXYLASE; 1.
DR   Pfam; PF02784; Orn_Arg_deC_N; 1.
DR   Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR   PRINTS; PR01181; DAPDCRBXLASE.
DR   PRINTS; PR01179; ODADCRBXLASE.
DR   SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_02120};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_02120};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02120};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW   Rule:MF_02120};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW   Rule:MF_02120}; Reference proteome {ECO:0000313|Proteomes:UP000008139}.
FT   DOMAIN          28..368
FT                   /note="Orn/DAP/Arg decarboxylase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00278"
FT   DOMAIN          33..278
FT                   /note="Orn/DAP/Arg decarboxylase 2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02784"
FT   ACT_SITE        341
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600183-50"
FT   BINDING         236
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         272..275
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         275
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         342
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         370
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120"
FT   MOD_RES         57
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02120,
FT                   ECO:0000256|PIRSR:PIRSR600183-50"
SQ   SEQUENCE   412 AA;  46203 MW;  987512021BC680EC CRC64;
     MFEYKNNELY AEGVRVKNIV DNVGSPVYVY SKGHFKAQFE KFNKAFSREH VIAFAIKSNS
     NLAVIKTFAS LGAGADIVSK GELFRAIKAG VDTSKIVFSG VAKRDDEIEY ALENDIMMIN
     VESEDELYNV NRVAEKLNKK ARIAFRVNPD VDPKTHPYIS TGLKKNKFGV PYEEAYDLYL
     KAKELKNIDV YGIQFHIGSQ LLDTTPIYDA SVRVADLMRR LTDKGVEFRV VDVGGGVGIV
     YDEKTDKEPD VNLYARQIEE AFRDFDVKLV LEPGRFLVGN GGILVSKVIY HKTNGQKNFL
     IIDAGMNDLL RPSLYKAYHK IAPMKKTGSK AIKCDIVGPI CETGDFFARD YEIEDVPNGN
     FIVVFSAGAY GFTMASNYNS RPRPAEVLVS GDSYRVVRER ESLEDLIKGE IL
//