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Database: UniProt
Entry: U2Z5D7_9RHOB
LinkDB: U2Z5D7_9RHOB
Original site: U2Z5D7_9RHOB 
ID   U2Z5D7_9RHOB            Unreviewed;       341 AA.
AC   U2Z5D7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=1-aminocyclopropane-1-carboxylate deaminase {ECO:0000313|EMBL:GAD56277.1};
GN   ORFNames=MBELCI_2329 {ECO:0000313|EMBL:GAD56277.1};
OS   Limimaricola cinnabarinus LL-001.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Limimaricola.
OX   NCBI_TaxID=1337093 {ECO:0000313|EMBL:GAD56277.1, ECO:0000313|Proteomes:UP000016566};
RN   [1] {ECO:0000313|EMBL:GAD56277.1, ECO:0000313|Proteomes:UP000016566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LL-001 {ECO:0000313|EMBL:GAD56277.1,
RC   ECO:0000313|Proteomes:UP000016566};
RA   Nishi S., Tsubouchi T., Takaki Y., Koyanagi R., Satoh N., Maruyama T.,
RA   Hatada Y.;
RT   "Draft Genome Sequence of Loktanella cinnabarina LL-001T, Isolated from
RT   Deep-Sea Floor Sediment.";
RL   Genome Announc. 1:e00927-13(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000256|ARBA:ARBA00008639}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAD56277.1}.
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DR   EMBL; BATB01000033; GAD56277.1; -; Genomic_DNA.
DR   RefSeq; WP_021694378.1; NZ_BATB01000033.1.
DR   AlphaFoldDB; U2Z5D7; -.
DR   STRING; 1337093.MBELCI_2329; -.
DR   eggNOG; COG2515; Bacteria.
DR   OrthoDB; 9801249at2; -.
DR   Proteomes; UP000016566; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR   PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR006278-2}.
FT   DOMAIN          11..318
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   ACT_SITE        76
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-1"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006278-2"
SQ   SEQUENCE   341 AA;  36654 MW;  732D7DC3A48BD6C0 CRC64;
     MHLARFPRVH LAHLPTPLER LDRLSAELGG PEIWIKRDDC TGLSTGGNKT RKLEFLMAEA
     QAMGADMVMT QGATQSNHAR QTAAFASKLG LRCHLLLEDR TGSKDHNYNR NGNVLLDHLH
     GATTETRGPD LDMHAEMETV ADTFRKDGKK VYTIPGGGSN ATGALGYVNC AFELVGQAND
     RGMVIDHIVT ATGSAGTQAG LITGLKAINA QIPLLGIGVR APREKQEENV YKLARLTAEK
     LGCEGVVARE DVIANCDYVG EGYGIPREDT IEAIRMFAEL EGILLDPVYS GKGAAGLIDQ
     IRKGRFKKGE RVVFLHTGGA AALFGYDAVF ECAPGDKLAA E
//
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