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 Q3IFT7

Entry ID Method Resolution Chain Position Source
AF-Q3IFT7-F1 Predicted AlphaFoldDB

No variants for Q3IFT7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3IFT7

No associated diseases with Q3IFT7

3 regional properties for Q3IFT7

Type Name Position InterPro Accession
domain Aldehyde dehydrogenase domain 12 - 462 IPR015590
conserved_site Aldehyde dehydrogenase, cysteine active site 273 - 284 IPR016160
conserved_site Aldehyde dehydrogenase, glutamic acid active site 245 - 252 IPR029510

Functions

Description
EC Number 1.2.1.71 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 GO annotations of molecular function

Name Definition
succinylglutamate-semialdehyde dehydrogenase activity Catalysis of the reaction: N-succinyl-L-glutamate 5-semialdehyde + H(2)O + NAD(+) = N-succinyl-L-glutamate + 2 H(+) + NADH.

2 GO annotations of biological process

Name Definition
arginine catabolic process to glutamate The chemical reactions and pathways resulting in the breakdown of arginine into other compounds, including glutamate.
arginine catabolic process to succinate The chemical reactions and pathways resulting in the breakdown of arginine into other compounds, including succinate.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTHPAQFING QWSQGQGTEF SSVNPANNNV IFQANSATAE QVDAAVSAAR EAFYAWADKT
70 80 90 100 110 120
FAERLEIVKA FAAQLKENSE ELAITIAQET GKPLWETRTE AGAMVGKIAI SEKAFLERTG
130 140 150 160 170 180
DVENAMPLGR AMIRHKPHGV VAVFGPYNFP GHLPNGHIVP ALLAGNTVIF KPSELTPKVA
190 200 210 220 230 240
ELTLKLWEKA GLPAGVINLV QGEVATGKAL AAHKGIDGLF FTGSSRTGHI LHEQFAGQPG
250 260 270 280 290 300
KILALEMGGN NPLIITDVED TKAVVHDIIQ SAFISSGQRC TCARKLFLPT GSKGDVILER
310 320 330 340 350 360
LITATKAIKV GNYDDADQPF MGSMISSAAA AGMVKAQNEL VELGAQVLVE LEHTVNTGFV
370 380 390 400 410 420
TPGIIECTNI SDFPDEEHFG PLLKVFRFDD FDQAIDKAND TSFGLSAGLL SDSAADYEHF
430 440 450 460 470 480
LRRIRAGIVN WNRPITGASS AAPFGGIGAS GNHRASAYYA ADYCAYPVAS VELEKVAMPA
TLSPGLKID