ID   Q9X592_NIVIR            Unreviewed;       432 AA.
AC   Q9X592;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   13-SEP-2023, entry version 72.
DE   SubName: Full=Pectate lyase {ECO:0000313|EMBL:AAD25394.1};
GN   Name=pelA {ECO:0000313|EMBL:AAD25394.1};
OS   Niveispirillum irakense (Azospirillum irakense).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Niveispirillum.
OX   NCBI_TaxID=34011 {ECO:0000313|EMBL:AAD25394.1};
RN   [1] {ECO:0000313|EMBL:AAD25394.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KBC1 {ECO:0000313|EMBL:AAD25394.1};
RX   PubMed=10198006;
RA   Bekri M.A., Desair J., Keijers V., Proost P., Searle-van Leeuwen M.,
RA   Vanderleyden J., vande Broek A.;
RT   "Azospirillum irakense produces a novel type of pectate lyase.";
RL   J. Bacteriol. 181:2440-2447(1999).
RN   [2] {ECO:0007829|PDB:1R76}
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-432, AND ACTIVE SITE.
RX   PubMed=15159558; DOI=10.1107/s090744490400602x;
RA   Novoa De Armas H., Verboven C., De Ranter C., Desair J., Vande Broek A.,
RA   Vanderleyden J., Rabijns A.;
RT   "Azospirillum irakense pectate lyase displays a toroidal fold.";
RL   Acta Crystallogr. D 60:999-1007(2004).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF121904; AAD25394.1; -; Genomic_DNA.
DR   PDB; 1R76; X-ray; 2.65 A; A=25-432.
DR   PDBsum; 1R76; -.
DR   AlphaFoldDB; Q9X592; -.
DR   SMR; Q9X592; -.
DR   CAZy; PL10; Polysaccharide Lyase Family 10.
DR   EvolutionaryTrace; Q9X592; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR012669; Pectate_lyase.
DR   NCBIfam; TIGR02474; pec_lyase; 1.
DR   Pfam; PF09492; Pec_lyase; 1.
DR   SUPFAM; SSF81853; Family 10 polysaccharide lyase; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:1R76}; Lyase {ECO:0000313|EMBL:AAD25394.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..432
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004336220"
FT   ACT_SITE        307
FT                   /note="EMO_00062 proton shuttle (general acid/base)"
FT                   /evidence="ECO:0007829|PDB:1R76"
FT   SITE            172
FT                   /note="EMO_00033 electrostatic stabiliser"
FT                   /evidence="ECO:0007829|PDB:1R76"
SQ   SEQUENCE   432 AA;  47007 MW;  A9E0F8D7ED0F2490 CRC64;
     MKRIALLIPL FASNLLIPAT VASAAVIGMN EAASALTPSR VSSLPDTQRA AWQEYLARSE
     AQLSRDKASL AAELAPGQPL PPPPAEGKGA DTMPLDKPAA WYTSKAARHV ADVIVSFQTP
     AGGWGKNQPR DGALRLPGQH YTGENVAKVK SGSNDLDAAR DRDWHYVGTI DNDATVTEIR
     FLAQVVSQLA PEEAAPYRDA ALKGIEYLLA SQFPNGGWPQ VWPLEGGYHD AITYNDDALV
     HVAELLSDIA AGRDGFGFVP PAIRTRALEA TNAAIHCIVE TQVVQDGKRL GWGQQHDALT
     LRPTSARNFE PAALSSTESA RILLFLMEIE APSDAVKQAI RGGVAWLNTS VIRDRAWVKS
     DQGYQLVTEQ GAKPLWSRFY SLDGNKPVFG DRDKTIHDDV MGISQERRTG YAWYTTSPQK
     ALSAFTKWEK RS
//