Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q6BZP5

Entry ID Method Resolution Chain Position Source
AF-Q6BZP5-F1 Predicted AlphaFoldDB

No variants for Q6BZP5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6BZP5

No associated diseases with Q6BZP5

2 regional properties for Q6BZP5

Type Name Position InterPro Accession
conserved_site Isocitrate lyase/phosphorylmutase, conserved site 236 - 241 IPR018523
domain ICL/PEPM domain 95 - 500 IPR039556

Functions

Description
EC Number 4.1.3.30 Oxo-acid-lyases
Subcellular Localization
  • Mitochondrion matrix
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.

2 GO annotations of molecular function

Name Definition
isocitrate lyase activity Catalysis of the reaction: isocitrate = glyoxylate + succinate.
methylisocitrate lyase activity Catalysis of the reaction: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate.

1 GO annotations of biological process

Name Definition
propionate catabolic process, 2-methylcitrate cycle The chemical reactions and pathways resulting in the breakdown of propionate that occurs in the 2-methylcitrate cycle.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLRTRFINSV NSARAMSRNI NTLSQFPYPT LQQEESFFKS QVEDIEKWWA SPRYEGIKRP
70 80 90 100 110 120
YTAEKVAIHR GTLPQTYASS VQAEKLFNIF TERGKQGLPV HTTGSVDPVQ MTQSAPHQEV
130 140 150 160 170 180
VYISGWACSS LLTTTNEVSP DFGDYPYDTV PNQVDRIFRA QGLHDKKAWH EWMSLSHEER
190 200 210 220 230 240
VKRDQEGKGR IDYLRPIIAD ADTGHGGLSA VMKLAKLFAE RGAAAIHLED QLHGGKKCGH
250 260 270 280 290 300
LAGKVIVPTG SHISRLNATR MQWDIMGCSN LVIARTDSES AKLLSSAADP SDHEYILGVV
310 320 330 340 350 360
KPIKPLAEVL LTAEANGATA DMVNKLELEW TKEAEMMTYD EAVQRALTEA GKSDKIEEYL
370 380 390 400 410 420
TKAKGKSNFE ARQIADELAG KHIFFDWDAP KTREGHYHVQ CGIEPAIKRA LAFAPYADLI
430 440 450 460 470 480
WLETKTPDLA QAQAFAKRIR EKFPGKWLVY NLSPSFNWSA HGYSDEQLKS FVWDLAKSGF
490 500 510 520 530 540
VMQLISLAGL HSNAVATHEL STRFKTEGMK AYVDLVQRKE KELGCDVLTH QKWSGANYLD
550 560
SIISTVQSGS SGTSSTGGDS TENQF